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Articles de revues sur le sujet « Proteinaceo »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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1

Oppert, B., K. Hartzer, and M. Zuercher. "Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae)." Bulletin of Entomological Research 92, no. 4 (2002): 331–36. http://dx.doi.org/10.1079/ber2002179.

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AbstractThe cigarette beetle, Lasioderma serricorne (Fabricius), is a common pest of stored foods. A study of digestive proteinases in L. serricorne was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. Optimal casein hydrolysis by luminal proteinases of L. serricorne was in pH 8.5–9.0 buffers, although the pH of luminal contents was slightly acidic. Results from substrate and inhibitor analyses indicated that the primary digestive proteinases were serine proteinases. The most effective inhibitors of caseinolytic hydrolysis were from soybea

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Jankangram, Wichuda, and Sunthorn Chooluck. "In silico Analysis and Characterization of a Putative Aspartic Proteinase Inhibitor, IA3 from Lachancea kluyveri." Trends in Sciences 20, no. 3 (2023): 6377. http://dx.doi.org/10.48048/tis.2023.6377.

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Aspartic proteinases play important role in various physiological and biological processes. Understanding catalytic mechanisms of these enzymes could lead to crucial medical and biological applications. Two types of aspartic proteinase inhibitors have been identified i.e. small molecule inhibitor and naturally occurring peptides. Most of aspartic proteinases are highly susceptible to inhibition by a series of small, non-proteinaceous natural products; pepstatin. However, only limited number of naturally-occurring polypeptide inhibitors of aspartic proteinases has so far been discovered. One am

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Rosenthal, P. J., K. Kim, J. H. McKerrow, and J. H. Leech. "Identification of three stage-specific proteinases of Plasmodium falciparum." Journal of Experimental Medicine 166, no. 3 (1987): 816–21. http://dx.doi.org/10.1084/jem.166.3.816.

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We have identified and characterized three stage-specific proteinases of Plasmodium falciparum that are active at neutral pH. We analyzed ring-, trophozoite-, schizont-, and merozoite-stage parasites by gelatin substrate PAGE and characterized the identified proteinases with class-specific proteinase inhibitors. No proteinase activity was detected with rings. Trophozoites had a 28 kD proteinase that was inhibited by inhibitors of cysteine proteinases. Mature schizonts had a 35-40 kD proteinase that also was inhibited by cysteine proteinase inhibitors. Merozoite fractions had a 75 kD proteinase

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Sever, Natasa, Metka Filipic, Joze Brzin, and Tamara T. Lah. "Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro." Biological Chemistry 383, no. 5 (2002): 839–42. http://dx.doi.org/10.1515/bc.2002.088.

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Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases redu

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Pandit, Shashi B., and N. Srinivasan. "Identification and Analysis of a New Family of Bacterial Serine Proteinases." In Silico Biology: Journal of Biological Systems Modeling and Multi-Scale Simulation 4, no. 4 (2004): 563–72. https://doi.org/10.3233/isb-00157.

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A family of hypothetical proteins, identified predominantly from archaeal genomes, has been analyzed in order to understand its functional characteristics. Using extensive sequence similarity searches it is inferred that this family is remotely related (best sequence identity is 19%) to ClpP proteinases that belongs to serine proteinase class. This family of hypothetical proteins is referred to as SDH proteinase family based on conserved sequential order of Ser, Asp and His residues and predicted serine proteinase activity. Results of fold recognition of SDH family sequences confirmed the remo

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Hiemstra, P. S. "Novel roles of protease inhibitors in infection and inflammation." Biochemical Society Transactions 30, no. 2 (2002): 116–20. http://dx.doi.org/10.1042/bst0300116.

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The local balance between proteinase inhibitors and proteinases determines local proteolytic activity. Various studies have demonstrated the importance of serine proteinase inhibitors in regulating the activity of serine proteinases that are released by leucocytes during inflammation. Recently it has been shown that these inhibitors may also display functions that are distinct from those associated with the inhibition of leucocyte-derived proteinases. In this review the results of selected studies focusing on three inhibitors of neutrophil elastase, i.e. α1-proteinase inhibitor, secretory leuc

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Ikeda, T. "Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187." Journal of Helminthology 77, no. 1 (2003): 21–26. http://dx.doi.org/10.1079/joh2002144.

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AbstractThe involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leu

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8

Bózner, P., and P. Demeš. "Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type." Parasitology 102, no. 1 (1991): 113–15. http://dx.doi.org/10.1017/s0031182000060418.

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SUMMARYHigh molecular weight proteinases ofTrichomonas vaginalis(with apparentMrvalues 142 and > 220 kDa) andTritrichomonas mobilensis(Mr67, 86, 104 and 120 kDa), optimally active at pH 8, were analysed in gelatin-containing polyacrylamide gels. All of these proteinases were resistant to serine-, aspartic- as well as cysteine proteinase inhibitors. Both proteolytic bands inT. vaginalisand two proteinases inT. mobilensis(67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase ofT. mobilensiswas inhibited also byo-phen

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9

Jakobs, K. H., and K. Aktories. "Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets." Biochemical Journal 249, no. 3 (1988): 639–43. http://dx.doi.org/10.1042/bj2490639.

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The influence of various proteinases on GTP hydrolysis was studied in membranes of human platelets. Of the proteinases examined, trypsin, acrosin and a recently described trypsin-like proteinase from bovine sperm, but not chymotrypsin, increased GTP hydrolysis. Similar to what was described previously for hormone-like agents, the stimulation of GTP hydrolysis by the proteinases was only observed at low GTP concentrations, with apparent Km values of 0.2-0.3 microM-GTP. Stimulation of the high-affinity GTPase by the proteinases occurred without apparent lag phase and was constant over a long per

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10

Garciacarreno, F. L., L. E. Dimes, and N. F. Haard. "Substrate-Gel Electrophoresis for Composition and Molecular Weight of Proteinases or Proteinaceous Proteinase Inhibitors." Analytical Biochemistry 214, no. 1 (1993): 65–69. http://dx.doi.org/10.1006/abio.1993.1457.

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Dubin, A., J. Potempa, and J. Travis. "Structural and functional characterization of elastases from horse neutrophils." Biochemical Journal 300, no. 2 (1994): 401–6. http://dx.doi.org/10.1042/bj3000401.

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In order better to understand the pathophysiology of the equine form of emphysema, two elastinolytic enzymes from horse neutrophils, referred to as proteinases 2A and 2B, have been extensively characterized and compared with the human neutrophil proteinases, proteinase-3 and elastase. Specificity studies using both the oxidized insulin B-chain and synthetic peptides revealed that cleavage of peptide bonds with P1 alanine or valine residues was preferred. Further characterization of the two horse elastases by N-terminal sequence and reactive-site analyses indicated that proteinases 2A and 2B ha

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12

Coppedge, B. R., J. M. Jones, G. W. Felton, and F. M. Stephen. "Examination of Midgut Proteinases of the Adult Southern Pine Beetle (Coleoptera: Scolytidae)." Journal of Entomological Science 29, no. 4 (1994): 457–65. http://dx.doi.org/10.18474/0749-8004-29.4.457.

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The midgut of adult southern pine beetles, Dendroctonus frontalis Zimmermann (Coleoptera: Scolytidae), contains digestive enzymes with optimal proteolytic activity in vitro near pH 7. General proteinase activity was significantly inhibited by serine and cysteine proteinase class inhibitors, while limited activation by cysteine proteinase class activators was apparent. These results indicate that both cysteine and serine proteinases are present in the adult midgut. The presence of both proteinase classes in adult southern pine beetles coincides with previous studies showing widespread occurrenc

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13

FERNÁNDEZ, J., A. F. MOHEDANO, P. GAYA, M. MEDINA, and M. NUÑEZ. "Purification and Characterization of Three Extracellular Proteinases Produced by Pseudomonas fluorescens INIA 745, an Isolate from Ewe's Milk." Journal of Food Protection 62, no. 5 (1999): 543–46. http://dx.doi.org/10.4315/0362-028x-62.5.543.

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Three proteinases were isolated from culture medium of Pseudomonas fluorescens INIA 745 and purified to homogeneity by a combination of Phenyl-Sepharose, DEAE-Sepharose, and Sephadex G-100 chromatography. Optimal temperature for enzymatic activity was 45°C for all three proteinases. The pH optimum of proteinases I and II was found to be 7.0, while that of proteinase III was 8.0. Divalent metal ions like Cu2+, Co2+, Zn2+, Fe2+, and Hg2+ were inhibitory to proteinase activity while Ca2+, Mg2+, and Mn2+ had little or no inhibitory effect. The three enzymes were strongly inhibited by EDTA and 1,10

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14

Todorova, V. K., D. P. Knox, and M. W. Kennedy. "Proteinases in the excretory/secretory products (ES) of adult Trichinella spiralis." Parasitology 111, no. 2 (1995): 201–8. http://dx.doi.org/10.1017/s0031182000064957.

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SUMMARYAdult Trichinella spiralis were maintained in vitro using defined media and the material excreted/secreted (ES) during this time examined for proteolytic enzyme (proteinase) activity using an azocasein assay and gelatin-substrate gels. Several discrete proteinases in the size range 14–100 kDa were observed with optimal activity at pH 7·5. The use of a class-differentiating panel of proteinase inhibitors indicated that serine proteinases were predominant although some inhibition was evident in the presence of cysteine and metalloproteinase inhibitors. Of a panel of potential natural prot

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15

St. Leger, Raymond J. "The role of cuticle-degrading proteases in fungal pathogenesis of insects." Canadian Journal of Botany 73, S1 (1995): 1119–25. http://dx.doi.org/10.1139/b95-367.

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The proteinaceous outer integument of insects forms an effective barrier against most microbes. Only the 700 known species of entomopathogenic fungi effect entry into their hosts by breaching the cuticle. There is accumulating evidence that the ability of fungi to degrade protein may aid their invasion of and growth in this orderly complex structure. Evidence for the particular importance of proteinases derives largely from studies of their production in infected cuticles associated with cuticle degradation, the effects of proteinase inhibitors on pathogen behavior, and by the analysis of prot

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16

Talbot, James A., Klaus Nielsen, and Lynette B. Corbeil. "Cleavage of proteins of reproductive secretions by extracellular proteinases of Tritrichomonas foetus." Canadian Journal of Microbiology 37, no. 5 (1991): 384–90. http://dx.doi.org/10.1139/m91-062.

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Cleavage of host defense proteins from reproductive secretions was investigated as a potential virulence mechanism for Tritrichomonas foetus extracellular proteinases. Three categories of susceptibility to digestion were found among the defense proteins tested. Cleavage of fibrinogen, fibronectin, and albumin occurred rapidly with more than 50% of these digested within 30 min. Lactoferrin, immunoglobulin G1, and immunoglobulin G2 were more than 50% digested after 4 h. Transferrin, immunoglobulin M, and immunoglobulin A were the most resistant to the Tritrichomonas foetus extracellular proteina

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D'AVILA-LEVY, C. M., F. M. ARAUJO, A. B. VERMELHO, R. M. A. SOARES, A. L. S. SANTOS, and M. H. BRANQUINHA. "Proteolytic expression inBlastocrithidia culicis: influence of the endosymbiont and similarities with virulence factors of pathogenic trypanosomatids." Parasitology 130, no. 4 (2004): 413–20. http://dx.doi.org/10.1017/s0031182004006705.

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Blastocrithidia culicisis an insect trypanosomatid that presents bacterial endosymbionts. The cell-associated and secreted proteinases of the endosymbiont-bearing and aposymbiotic strains were compared through the incorporation of proteinaceous substrates into sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Few qualitative changes could be detected in the proteolytic zymograms in the 2 strains studied when gelatin, casein, haemoglobin or bovine serum albumin (BSA) were tested. However, the level of proteolytic activities was significantly higher in the aposymbiotic strain

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18

Mills, J. S. "Virus Proteinase Inhibitors — What Next after HIV?" Antiviral Chemistry and Chemotherapy 7, no. 6 (1996): 281–93. http://dx.doi.org/10.1177/095632029600700601.

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The recent approval by the regulatory authorities in the United States of several HIV proteinase inhibitors as therapeutics for the treatment of AIDS confirms that virus proteinases are valid molecular targets in the search for new antiviral drugs. This review summarizes the available approaches that can be taken to discover virus proteinase inhibitors and reviews the current status of our knowledge with respect to virus proteinases in viruses of clinical significance other than HIV. The major focus is on proteinases identified in the viruses that cause the common cold, hepatitis C virus and t

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Hortin, Glen L., Ilka Warshawsky, and Maryline Laude-Sharp. "Macromolecular Chromogenic Substrates for Measuring Proteinase Activity." Clinical Chemistry 47, no. 2 (2001): 215–22. http://dx.doi.org/10.1093/clinchem/47.2.215.

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Abstract Background: Proteinase activities are often measured using chromogenic substrates that are much smaller than physiological substrates. Methods: The hydrodynamic size of macromolecular substrates (macrosubstrates) prepared by linking small chromogenic substrates to polyethylene glycol was determined by gel filtration. Efficiency of macrosubstrate cleavage by proteinases and α2-macroglobulin-proteinase complexes was monitored spectrophotometrically. Results: Macrosubstrates had hydrodynamic radii of ∼20 Å, similar to proteins with a molecular weight of 18 000. Different macrosubstrates

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Jean, D., J. Hermann, F. Rodrigues-Lima, M. Barel, M. Balbo, and R. Frade. "Identification on melanoma cells of p39, a cysteine proteinase that cleaves C3, the third component of complement: amino-acid-sequence identities with procathepsin L." Biochemical Journal 312, no. 3 (1995): 961–69. http://dx.doi.org/10.1042/bj3120961.

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We previously identified, on normal or tumour cells, two membrane proteinases, p57 and p65, that cleave human C3, the third component of complement, thus regulating C3′s biological properties. Whereas p57 was purified from human erythrocytes, p65 was identified using polyclonal anti-p57 antibodies on a human melanoma cell line resistant to complement lysis. Analysis of cell distribution of C3-cleaving proteinases established that DSm, a murine melanoma cell line, expressed a C3-cleaving proteinase distinct from p57 and p65 proteinases. Thus we purified the C3-cleaving proteinase solubilized fr

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Kang, Yoon-Suk, Young-Bae Chun, and Moon-Jae Cho. "Purification and Characterization of proteinase from Ruditapes philippinarum infected with Perkinsus sp." Journal of Medicine and Life Science 1, no. 1 (2003): 53–56. http://dx.doi.org/10.22730/jmls.2003.1.1.53.

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In this study, we characterized a proteinase from marine bivalve Ruditapes philippinarum (Manila clam) infected with the protozoan parasite Perkinsus sp. When infected with Perkinsus sp., Manila clam produced a proteinase, which was not appeared in non-infected manila clam and Perkinsus hypnospore. A clear baiid of 45 kDa was detected on 0.2% gelatin containing gel SDS-PAGE. The proteinase was inhibited by phenylmethyl sulfonyl fluoride (PMSF) known as a serine proteinase inhibitor. Using Mucin-Sepharose CL-6B affinity chromatography, proteinases were eluted by Tris-HCl buffer (pH 7.4) contain

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Takeuchi, K., H. Wood, and R. T. Swank. "Lysosomal elastase and cathepsin G in beige mice. Neutrophils of beige (Chediak-Higashi) mice selectively lack lysosomal elastase and cathepsin G." Journal of Experimental Medicine 163, no. 3 (1986): 665–77. http://dx.doi.org/10.1084/jem.163.3.665.

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A profound decrease in activities of the two lysosomal serine proteinases, elastase, and cathepsin G, was found in neutrophils of four independent beige mutants. Elastase and cathepsin G activities were assayed with the specific synthetic substrates MeO-Suc-Ala-Ala-Pro-Val-MCA and Suc-Ala-Ala-Pro-Phe-pNA, respectively. The defect is intrinsic to cells of beige mice, since transplantation of bone marrow from normal to mutant mice restored normal proteinase activity, and normal mice transplanted with beige marrow produced neutrophils with a deficiency of proteinase activity. The loss of elastase

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Manocha, M. S., and R. Balasubramanian. "In vitro regulation of chitinase and chitin synthase activity of two mucoraceous hosts of a mycoparasite." Canadian Journal of Microbiology 34, no. 10 (1988): 1116–21. http://dx.doi.org/10.1139/m88-197.

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Effects of partially purified preparations of proteinases extracted from Choanephora cucurbitarum and Phascolomyces articulosus, susceptible and resistant hosts of Piptocephalis virginiana, respectively, were studied in vitro on the activities of chitinase and chitin synthase of the same hosts. Both chitinase and chitin synthase are membrane bound, zymogenic, and activated by partial proteolysis. Host proteinases of acid and neutral type stimulated chitinase activity, but only the acid proteinase stimulated chitin synthase activity of the two hosts. Neutral proteinase of C. cucurbitarum inhibi

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Peng, Chih-Wen, Valera V. Peremyslov, Arcady R. Mushegian, William O. Dawson, and Valerian V. Dolja. "Functional Specialization and Evolution of Leader Proteinases in the Family Closteroviridae." Journal of Virology 75, no. 24 (2001): 12153–60. http://dx.doi.org/10.1128/jvi.75.24.12153-12160.2001.

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ABSTRACT Members of the Closteroviridae andPotyviridae families of the plant positive-strand RNA viruses encode one or two papain-like leader proteinases. In addition to a C-terminal proteolytic domain, each of these proteinases possesses a nonproteolytic N-terminal domain. We compared functions of the several leader proteinases using a gene swapping approach. The leader proteinase (L-Pro) of Beet yellows virus (BYV; a closterovirus) was replaced with L1 or L2 proteinases of Citrus tristeza virus (CTV; another closterovirus), P-Pro proteinase of Lettuce infectious yellows virus (LIYV; a criniv

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MORADIAN-OLDAK, Janet, Wendy LEUNG, James P. SIMMER, Margarita ZEICHNER-DAVID, and Alan G. FINCHAM. "Identification of a novel proteinase (ameloprotease-I) responsible for the complete degradation of amelogenin during enamel maturation." Biochemical Journal 318, no. 3 (1996): 1015–21. http://dx.doi.org/10.1042/bj3181015.

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During enamel formation the proteins of the extracellular matrix, particularly amelogenins, are removed prior to maturation. In order to investigate this process and to improve our understanding of the function of proteinases during enamel maturation, proteinase fractions were isolated from developing pig enamel and assayed for proteolytic activity in vitro. A recombinant murine amelogenin, M179, was used as a substrate. Two major groups of enamel proteinases were defined as high-molecular-mass [‘high-molecular-weight’ in Moradian-Oldak, Simmer, Sarte, Zeichner-David and Fincham (1994) Arch. O

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Rymerson, Robert T., and Robert P. Bodnaryk. "GUT PROTEINASE ACTIVITY IN INSECT PESTS OF CANOLA." Canadian Entomologist 127, no. 1 (1995): 41–48. http://dx.doi.org/10.4039/ent12741-1.

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AbstractThe digestive proteinases of three important pests of canola, Brassica napus L. and B. rapa L., in western Canada were characterized by assessing the proteolytic activity of homogenates of their midguts against azocasein or azoalbumin at various pH levels and in the presence of diagnostic proteinase inhibitors. The midgut of larvae of the bertha armyworm, Mamestra configurata Wlk., had maximum proteolytic activity at pH 10.5 which was inhibited 45–60% by serine proteinase inhibitors such as the soybean trypsin inhibitor. The midgut of larvae of the diamondback moth, Plutella xylostella

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Ikeda, T. "Protein A immunocapture assay detecting antibodies to fluke cysteine proteinases for immunodiagnosis of human paragonimiasis and fascioliasis." Journal of Helminthology 75, no. 3 (2001): 245–49. http://dx.doi.org/10.1079/joh200161.

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Enzyme-linked immunosorbent assays (ELISAs) which detect specific antibodies to fluke cysteine proteinases have provided good sensitivity and specificity for the immunodiagnosis of trematode diseases. To detect specific antibodies without the need for purified proteinase antigens, an immunocapture assay using Protein A was applied for the immunodiagnosis of paragonimiasis and fascioliasis. ELISA plate wells were coated with Protein A, incubated with diluted patient sera, then incubated with a preparation containing fluke cysteine proteinases, excretory–secretory (ES) products of adult Paragoni

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Fang, Weihuan, and Markus Sandholm. "Inhibition of the proteinase activity in mastitic milk." Journal of Dairy Research 62, no. 1 (1995): 61–68. http://dx.doi.org/10.1017/s0022029900033677.

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SummaryThe antiproteolytic activity of selected proteinase inhibitors was studied in mastitic bovine milk and urokinase-activated normal milk using a caseolytic agar diffusion assay. The inhibition profiles of mastitic milk and urokinase-activated milk were compared with those of purified proteinases. The proteinase inhibition profile of mastitic milk did not resemble that of any of the pure proteinases, indicating a mixed type of proteinase system in mastitic milk. The trypanocidals diminazene (equivalent to Berenil®) and pentamidine (equivalent to Lomidine®), together with aprotinin (Trasylo

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Michaud, Dominique, Thierry C. Vrain, and Hugh A. Daubeny. "Potential of Plant Cystatins for the Production of Transgenic Strawberry Plants Resistant to the Black Vine Weevil." HortScience 30, no. 4 (1995): 828D—828. http://dx.doi.org/10.21273/hortsci.30.4.828d.

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Transformation of plant genomes with cysteine proteinase inhibitor (cystatin) genes represents an attractive option for the biological control of insect pests. However, this strategy must be carefully considered, because the transgenic plant endogenous proteinases may represent potential target enzymes for the exogenous inhibitors produced. For example, we are considering the transformation of strawberry (Fragaria ×ananassa) with cystatin cDNA clones, to control the Coleoptera pest black vine weevil (BVW; Otiorynchus sulcatus). Electrophoretic analyses of adult BVW proteinases have revealed th

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Goodenough, Peter W., Peter J. Kilshaw, Fiona McEwan, and A. Jane Owen. "Monoclonal antibodies to the two most basic papaya proteinases." Bioscience Reports 6, no. 8 (1986): 759–66. http://dx.doi.org/10.1007/bf01116544.

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The proteinases from Carica papaya include papain, isoenzymes of chymopapain and two proteinases A and B distinguished by their unusually high pI. The identity of one of the most basic proteinases has been questioned. The present report describes the preparation and characterisation of two monoclonal antibodies that react specifically with papaya proteinases A and B respectively and a third that identifies a common structural feature found in papain and proteinase A.

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Thøgersen, I. B., G. Salvesen, F. H. Brucato, S. V. Pizzo та J. J. Enghild. "Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris". Biochemical Journal 285, № 2 (1992): 521–27. http://dx.doi.org/10.1042/bj2850521.

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The cell-free haemolymph of the mollusc Octopus vulgaris inhibited the proteolytic activity of the thermolysin against the high-molecular-mass substrate hide powder azure. The purified inhibitor was a glycoprotein composed of two identical 180 kDa disulphide-linked subunits. In addition to the inhibition of the metalloproteinase thermolysin, the protein inhibited the serine proteinases human neutrophil elastase, pig pancreatic elastase, bovine chymotrypsin, bovine trypsin and the cysteine proteinase papain. A fraction of the proteinase-inhibitor complex resisted dissociation after denaturation

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Sinden, Nicola J., Michael J. Baker, David J. Smith, Jan-Ulrich Kreft, Timothy R. Dafforn та Robert A. Stockley. "α-1-Antitrypsin variants and the proteinase/antiproteinase imbalance in chronic obstructive pulmonary disease". American Journal of Physiology-Lung Cellular and Molecular Physiology 308, № 2 (2015): L179—L190. http://dx.doi.org/10.1152/ajplung.00179.2014.

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The excessive activities of the serine proteinases neutrophil elastase and proteinase 3 are associated with tissue damage in chronic obstructive pulmonary disease. Reduced concentrations and/or inhibitory efficiency of the main circulating serine proteinase inhibitor α-1-antitrypsin result from point mutations in its gene. In addition, α-2-macroglobulin competes with α-1-antitrypsin for proteinases, and the α-2-macroglobulin-sequestered enzyme can retain its catalytic activity. We have studied how serine proteinases partition between these inhibitors and the effects of α-1-antitrypsin mutation

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Lecaille, F., D. Muno, E. Kominami, and K. Ishidoh. "Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages." Biological Chemistry 385, no. 6 (2004): 511–16. http://dx.doi.org/10.1515/bc.2004.060.

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Abstract The mammalian legumain is a recently identified lysosomal cysteine proteinase belonging to the clan CD and homologous to plant legumain. This enzyme has the characteristic of specifically hydrolyzing peptide bonds after asparagine residues. As in the case of papain-type cysteine proteinases, legumain is synthesized as an inactive zymogen, and processed into a mature form localized in lysosomes. However, the mechanism of its activation remains unclear. In this study, we analyze which types of proteinases may participate in the processing of legumain in rat primary cultured macrophages

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Petersen, C. M., E. Ejlersen, S. K. Moestrup, P. H. Jensen, O. Sand, and L. Sottrup-Jensen. "Immunosuppressive properties of electrophoretically "slow" and "fast" form alpha 2-macroglobulin. Effects on cell-mediated cytotoxicity and (allo-) antigen-induced T cell proliferation." Journal of Immunology 142, no. 2 (1989): 629–35. http://dx.doi.org/10.4049/jimmunol.142.2.629.

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Abstract Lymphokine activated killer cell lysis of K562 cells was inhibited by alpha 2-macroglobulin (alpha 2M), soybean trypsin inhibitor, and alpha 1-proteinase inhibitor. In serum free medium 2 mg/ml alpha 2M suppressed target cell lysis in a 4-h cytotoxic assay with about 40%. Suppression was dose and time dependent. Cytotoxicity was unaffected by alpha 2M concentrations less than 0.25 mg/ml, and by alpha 2M added later than 1.5 h from start of assay. Pre-treatment of effector (but not of target) cells with alpha 2M was even more suppressive than the presence of alpha 2M during assay. Cell

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Knight, Kenneth R., Rakesh K. Khazanchi, W. Christopher Pederson, John J. McCann, Serena A. Coe, and Bernard McC O'Brien. "Coumarin and 7-Hydroxycoumarin Treatment of Canine Obstructive Lymphoedema." Clinical Science 77, no. 1 (1989): 69–76. http://dx.doi.org/10.1042/cs0770069.

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1. Canine obstructive lymphoedema was created in one hind leg of 30 dogs by irradiation of the groin and surgical removal of surviving lymph glands and lymphatics. The opposite leg served as a control. Once the oedema had stabilized, groups of 10 dogs were treated orally with 12.5 mg day−1 kg−1 for 8 months with either one of the benzopyrones coumarin (2H-1-benzopyran-2-one) and 7-hydroxycoumarin (7-hydroxy-2H-1-benzopyran-2-one), or placebo. 2. The two benzopyrones significantly (P < 0.01) but gradually reduced the oedema by 20–30% over 8 months, as judged by circumferential measurements o

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Nagy, L., B. R. Johnson, P. Hauschka, and S. Szabo. "Characterization of proteases and protease inhibitors in the rat stomach." American Journal of Physiology-Gastrointestinal and Liver Physiology 272, no. 5 (1997): G1151—G1158. http://dx.doi.org/10.1152/ajpgi.1997.272.5.g1151.

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Previously our laboratory reported increased activity of the thiol proteinase cathepsin B in gastric juice after ethanol-induced mucosal injury. In this study we measured proteinase activity (PA) and proteinase inhibitory activity (PIA) with the general substrates hemoglobin, azocasein, and bovine serum albumin (BSA) at optimal pH (2.0, 5.6, and 7.4) of aspartic, cysteine, and serine proteinases. Homogenates of glandular stomach mucosa and gastric juice from fasted rats were incubated in the presence or absence of specific inhibitors and sulfhydryl (SH) alkylators N-ethylmaleimide and iodoacet

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Koritsas, V. M., and H. J. Atkinson. "Proteinases of females of the phytoparasite Globodera pallida (potato cyst nematode)." Parasitology 109, no. 3 (1994): 357–65. http://dx.doi.org/10.1017/s0031182000078392.

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SummarySensitive assays capable of detecting proteinases in single females of the phytoparasite Globodera pallida have been developed and used to define the proteinase activity of young adult females. Digestion of the large subunit of the plant protein Rubisco established a pH optimum for the proteinase activity at pH 5·7. The activity was inhibited by the cysteine proteinase inhibitors p-chloromercuribenzoic acid (PMBA) and p-chloromercurisulphonic acid (PMSA) and stimulated by both cysteine and dithiothreitol (DTT). It was moderately reduced by L-trans-epoxysuccinyl-leucylamido-(4- guanidino

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GARCÍA-CARREÑO, F. L., M. A. NAVARRETE DEL TORO, M. DÍAZ-LÓPEZ, M. P. HERNÁNDEZ-CORTÉS, and J. M. EZQUERRA. "Proteinase Inhibition of Fish Muscle Enzymes Using Legume Seed Extracts." Journal of Food Protection 59, no. 3 (1996): 312–18. http://dx.doi.org/10.4315/0362-028x-59.3.312.

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Seed extracts from indigenous and introduced legumes were prepared and used to search for inhibitors of fish muscle proteinases. Fish flesh extracts were prepared from samples of Merluccius productus (Pacific whiting or merluza) obtained off the Oregon coast and in the Gulf of California, respectively. The proteinase activity in the fish muscle for the Pacific whiting was the highest, followed by parasitized merluza. The lowest proteinase activity was for the nonparasitized merluza. Six out of 12 seed extracts reduced the proteinase activity from the fish flesh by more than 50%. The reduction

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Buttle, D. J., A. A. Kembhavi, S. L. Sharp, R. E. Shute, D. H. Rich, and A. J. Barrett. "Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex." Biochemical Journal 261, no. 2 (1989): 469–76. http://dx.doi.org/10.1042/bj2610469.

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A procedure is described for the purification of a previously undetected cysteine proteinase, which we have called papaya proteinase IV, from spray-dried latex of the papaya (Carica papaya) plant. The purification involves affinity chromatography on Gly-Phe-aminoacetonitrile linked to CH-Sepharose 4B, with elution by 2-hydroxyethyl disulphide at pH 4.5. The product thus obtained is a mixture of almost fully active papain and papay proteinase IV, which are then separated by cation-exchange chromatography. A preliminary characterization of papaya proteinase IV showed it to be very similar to chy

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Folco, E. J. E., L. Busconi, C. B. Martone, and J. J. Sánchez. "Fish skeletal muscle contains a novel serine proteinase with an unusual subunit composition." Biochemical Journal 263, no. 2 (1989): 471–75. http://dx.doi.org/10.1042/bj2630471.

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Proteinase I, an enzyme previously shown to be able to degrade contractile and cytoskeletal elements of white-croaker (Micropogon opercularis) myofibrils, was purified to apparent homogeneity by chromatography on DEAE-Sephacel, octyl-Sepharose CL 4B and arginine-Sepharose 4B. Its Mr was determined to be 269,000 by Sephacryl S-300 gel filtration. Under denaturing conditions, the enzyme dissociated into two subunits with Mr 20,000 and 15,500, in a molar ratio of 1.8:1. Proteinase I showed a pH optimum of 8.5. The enzyme was strongly inhibited by several serine proteinase inhibitors, whereas inhi

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Buist, Girbe, Gerard Venema, and Jan Kok. "Autolysis of Lactococcus lactis Is Influenced by Proteolysis." Journal of Bacteriology 180, no. 22 (1998): 5947–53. http://dx.doi.org/10.1128/jb.180.22.5947-5953.1998.

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ABSTRACT The autolysin AcmA of Lactococcus lactis was shown to be degraded by the extracellular lactococcal proteinase PrtP. Autolysis, as evidenced by reduction in optical density of a stationary-phase culture and concomitant release of intracellular proteins, was greatly reduced when L. lactis MG1363 cells expressed the cell wall-anchored lactococcal proteinase PrtP of the PI-type caseinolytic specificity (PI). On the other hand, lactococcal strains that did not produce the proteinase showed a high level of autolysis, which was also observed when the cells produced the secreted form of PI or

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Stepanov, V. M., G. N. Rudenskaya, L. P. Revina, et al. "A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins." Biochemical Journal 285, no. 1 (1992): 281–86. http://dx.doi.org/10.1042/bj2850281.

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A homogeneous serine proteinase secreted by the extreme halophilic bacterium Halobacterium mediterranei 1538 was isolated by affinity chromatography on bacitracin-Sepharose with a yield of 48% (260-fold purification). The enzyme reveals an optimum for pyroglutamyl-Ala-Ala-Leu p-nitroanilide hydrolysis at pH 8.0-8.5 (Km 0.14 mM; k(cat). 36.9 s-1). Its activity increases linearly with NaCl concentration over the range 2-5 M. The substrate specificity of the enzyme is comparable with that of secretory subtilisins, the extent of protein degradation approaching that attained with proteinase K. The

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Dreyer, T., M. J. Valler, J. Kay, P. Charlton, and B. M. Dunn. "The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae)." Biochemical Journal 231, no. 3 (1985): 777–79. http://dx.doi.org/10.1042/bj2310777.

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The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The inhibitor appeared to be completely selective in that only the aspartic proteinase A from yeast was inhibited to any significant extent. IA3 thus represents the first example of a totally specific, naturally occurring, aspartic-proteinase inhibitor.

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Bartlett, J. D., and J. P. Simmer. "Proteinases in Developing Dental Enamel." Critical Reviews in Oral Biology & Medicine 10, no. 4 (1999): 425–41. http://dx.doi.org/10.1177/10454411990100040101.

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For almost three decades, proteinases have been known to reside within developing dental enamel. However, identification and characterization of these proteinases have been slow and difficult, because they are present in very small quantities and they are difficult to purify directly from the mineralizing enamel. Enamel matrix proteins such as amelogenin, ameloblastin, and enamelin are cleaved by proteinases soon after they are secreted, and their cleavage products accumulate in the deeper, more mature enamel layers, while the full-length proteins are observed only at the surface. These result

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Bózner, P., A. Gombošová, M. valent, P. Demeš, and J. F. Alderete. "Proteinases ofTrichomonas vaginalis: antibody response in patients with urogenital trichomoniasis." Parasitology 105, no. 3 (1992): 387–91. http://dx.doi.org/10.1017/s0031182000074552.

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SUMMARYImmunoprecipitation combined with electrophoresis in gelatin-polyacrylamide gels was successfully used for detection of antibodies against numerous proteinases ofTrichomonas vaginalisin infected patients. The method proved to be highly specific as anti-proteinase antibodies were absent in women with negative cultivation ofT. vaginalisand no history of trichomoniasis. Sera of 71% and vaginal washes of 86% patients with trichomoniasis were positive for these antibodies. In vaginal washes, but not in sera, antibodies were partly complexed with proteinases, possibly of trichomonad origin. I

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North, M. J., K. I. Scott, and B. C. Lockwood. "Multiple cysteine proteinase forms during the life cycle of Dictyostelium discoideum revealed by electrophoretic analysis." Biochemical Journal 254, no. 1 (1988): 261–68. http://dx.doi.org/10.1042/bj2540261.

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Proteinases of the cellular slime mould Dictyostelium discoideum have been analysed using electrophoresis on polyacrylamide gels containing gelatin (gelatin/PAGE). Multiple proteinase forms were apparent in vegetative myxamoebae, but the presence of individual enzyme forms depended on the manner in which the cells were grown. Axenic cells had a characteristic A-pattern of proteinases consisting of six bands, the most active enzymes having apparent Mr values of 51,000 and 45,000 (these have been named ddCP51 and ddCP45, respectively). Some of the proteinases were also present in the medium, the

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Elden, T. C. "Influence of a Cysteine Proteinase Inhibitor on Alfalfa Weevil (Coleoptera: Curculionidae) Growth and Development Over Successive Generations." Journal of Entomological Science 35, no. 1 (2000): 70–76. http://dx.doi.org/10.18474/0749-8004-35.1.70.

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The influence of leupeptin, a cysteine and serine proteinase inhibitor, on alfalfa weevil, Hypera postica (Gyllenhal), growth and development was investigated over nine successive generations. Concern that ingestion of proteinase inhibitors by phytophagous insects could induce production of inhibitor-insensitive proteinase activity initiated this investigation. The percent alfalfa weevil larval, pupal and adult survival, and defoliation was significantly lower on alfalfa foliage treated with leupeptin than on untreated foliage in all nine generations tested. Main effects for generations and tr

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LALMANACH, Gilles, Roger MAYER, Carole SERVEAU, Julio SCHARFSTEIN, and Francis GAUTHIER. "Biotin-labelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi." Biochemical Journal 318, no. 2 (1996): 395–99. http://dx.doi.org/10.1042/bj3180395.

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Biotin-labelled peptidyl diazomethane inhibitors of cysteine proteinases, based on the N-terminal substrate-like segment of human cystatin C, a natural inhibitor of cysteine proteinases, were synthesized. These synthetic derivatives were tested as irreversible inhibitors of cruzipain, the major cysteine proteinase of Trypanosoma cruzi, to compare the kinetics of the inhibition of the parasite proteinase with that of the mammalian cathepsins B and L. The accessibility of the active sites of these proteinases to these probes was also investigated. The inhibition of cruzipain by Biot-LVG-CHN2 (wh

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Knox, D. P., D. L. Redmond, and D. G. Jones. "Characterization of proteinases in extracts of adultHaemonchus contortus, the ovine abomasal nematode." Parasitology 106, no. 4 (1993): 395–404. http://dx.doi.org/10.1017/s0031182000067147.

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SUMMARYThe degradation of several protein substrates, including the blood proteins haemoglobin, albumin and fibrinogen, by proteinases present in extracts of adultHaemonchus contortuswas examined over a broad pH range. These proteinases were further characterized on the basis of substrate specificity, inhibitor sensitivity and molecular size by spectrophotometric and substrate gel analysis. The majority of the proteinases capable of degrading the blood proteins tested were active at acidic pH and could be ascribed to the cysteine proteinase class. In addition, evidence is presented that these

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North, M. J. "A bacterial factor induces changes in cysteine proteinase forms in the cellular slime mould Dictyostelium discoideum." Biochemical Journal 254, no. 1 (1988): 269–75. http://dx.doi.org/10.1042/bj2540269.

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The electrophoretic pattern of cysteine proteinases in axenically grown myxamoebae of Dictyostelium discoideum can be altered by the addition of either Gram-negative (Klebsiella aerogenes, Escherichia coli) or Gram-positive (Micrococcus lysodeikticus, Bacillus subtilis) bacteria to the culture. No changes occurred, however, if either yeast or latex beads were used in place of bacteria. The changes involved the simultaneous loss of proteinases characteristic of the axenic cells (the A-forms) and the acquisition of those found in cells which have been grown on bacteria (the B-forms). Using K. ae

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