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Journal articles on the topic 'Chromogenic substrates'

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Published: 4 June 2021
Last updated: 19 February 2022

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1

Hutton, R. A. "Chromogenic substrates in haemostasis." Blood Reviews 1, no. 3 (September 1987): 201–6. http://dx.doi.org/10.1016/0268-960x(87)90036-1.

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2

Burrous, Mary R., and John Westley. "Chromogenic substrates for sulfurtransferases." Analytical Biochemistry 149, no. 1 (August 1985): 66–71. http://dx.doi.org/10.1016/0003-2697(85)90477-4.

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3

Hortin, Glen L., Ilka Warshawsky, and Maryline Laude-Sharp. "Macromolecular Chromogenic Substrates for Measuring Proteinase Activity." Clinical Chemistry 47, no. 2 (February 1, 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 served as efficient substrates for chymotrypsin, trypsin, and thrombin. Linking small substrates to a polymer variably affected substrate efficiency, with the impact on activity ranging from a 60-fold decrease to a 30-fold increase. Proteinases complexed with α2-macroglobulin had ∼10-fold lower activity vs macrosubstrates than small substrates. Conclusions: Macrosubstrates are efficient substrates that allow decreased measurement of sterically hindered proteinase molecules such as α2-macroglobulin-proteinase complexes. Thus, macrosubstrates may provide more accurate functional assays of proteinases such as coagulation factors.
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4

Johnson, Gary M., and Robert Schaeper. "Chromogenic Lactate−Leukocyte Esterase Substrates." Bioconjugate Chemistry 8, no. 1 (January 1997): 76–80. http://dx.doi.org/10.1021/bc960081h.

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5

Marmuse, Laurence, Michèle Asther, David Navarro, Laurence Lesage-Meessen, Marcel Asther, Sébastien Fort, and Hugues Driguez. "Chromogenic substrates for feruloyl esterases." Carbohydrate Research 342, no. 15 (November 2007): 2316–21. http://dx.doi.org/10.1016/j.carres.2007.06.004.

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6

Conyers, Susan M., and David A. Kidwell. "Chromogenic substrates for horseradish peroxidase." Analytical Biochemistry 192, no. 1 (January 1991): 207–11. http://dx.doi.org/10.1016/0003-2697(91)90208-b.

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7

Marmuse, Laurence, Michèle Asther, Emeline Fabre, David Navarro, Laurence Lesage-Meessen, Marcel Asther, Michael O'Donohue, Sébastien Fort, and Hugues Driguez. "New chromogenic substrates for feruloyl esterases." Organic & Biomolecular Chemistry 6, no. 7 (2008): 1208. http://dx.doi.org/10.1039/b717742a.

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8

Somorin, O., W. Okiei, T. Emokpae, and M. Ogunlesi. "New lysine chromogenic substrates for trypsin." International Journal of Biological Macromolecules 9, no. 1 (February 1987): 27–31. http://dx.doi.org/10.1016/0141-8130(87)90021-3.

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9

Bozic, Natasa, Biljana Dojnov, Aleksandra Milovanovic, Vera Nenadovic, Jelisaveta Ivanovic, and Z. Vujcic. "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae." Archives of Biological Sciences 60, no. 3 (2008): 403–9. http://dx.doi.org/10.2298/abs0803403b.

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Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities.
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10

Mašková, Hana P., George Kokotos, Chryssa Tzougraki, and Tomislav Barth. "Synthesis and use of an aminoquinolinone derivative for the fluorometric determination of oxytocinase." Collection of Czechoslovak Chemical Communications 54, no. 10 (1989): 2802–8. http://dx.doi.org/10.1135/cccc19892802.

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A new fluorogenic substrate for the determination of the activity of human serum oxytocinase-cystine aminopeptidase (EC 3.4.11.3), H-Cys(Bzl)-NH-Meq, has been synthesized. The affinity of H-Cys(Bzl)-NH-Meq to oxytocinase was by two orders higher than that of the usually employed chromogenic substrates. The Michaelis constant of oxytocinase for this substrate was within the range of the optimum pH (7.0–7.5) 2.3.10-6 mol l-1, i.e. in the region of the affinity of the natural substrate, oxytocin. The concentration of dimethylsulfoxide used for the solubilization of H-Cys(Byl)-NH-Meq (<0.4%) did not influence adversely the course of the enzyme reaction as in the case of chromogenic substrates, where the concentrations of the organic solvent exceeded 3%.
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11

Budzynski, Andrei Z. "Chromogenic Substrates in Coagulation and Fibrinolytic Assays." Laboratory Medicine 32, no. 7 (July 1, 2001): 365–68. http://dx.doi.org/10.1309/kvym-1c8e-y6m4-mjdy.

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12

Chibba, Anthony, Somnath Dasgupta, Nandadeva Yakandawala, Srinivasa Madhyastha, and Mark Nitz. "Chromogenic Carbamate and Acetal Substrates for Glycosaminidases." Journal of Carbohydrate Chemistry 30, no. 7-9 (September 1, 2011): 549–58. http://dx.doi.org/10.1080/07328303.2011.610543.

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13

Grognux, Johann, Denis Wahler, Erich Nyfeler, and Jean-Louis Reymond. "Universal chromogenic substrates for lipases and esterases." Tetrahedron: Asymmetry 15, no. 18 (September 2004): 2981–89. http://dx.doi.org/10.1016/j.tetasy.2004.07.059.

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14

Dang, Quoc D., and Enrico Di Cera. "Chromogenic Substrates Selective for Activated Protein C." Blood 89, no. 6 (March 15, 1997): 2220–21. http://dx.doi.org/10.1182/blood.v89.6.2220.

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15

Wu, Xinghua, Yu Chen, Herve Aloysius, and Longqin Hu. "A novel high-yield synthesis of aminoacyl p-nitroanilines and aminoacyl 7-amino-4-methylcoumarins: Important synthons for the synthesis of chromogenic/fluorogenic protease substrates." Beilstein Journal of Organic Chemistry 7 (July 27, 2011): 1030–35. http://dx.doi.org/10.3762/bjoc.7.117.

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Aminoacyl p-nitroaniline (aminoacyl-pNA) and aminoacyl 7-amino-4-methylcoumarin (aminoacyl-AMC) are important synthons for the synthesis of chromogenic/fluorogenic protease substrates. A new efficient method was developed to synthesize aminoacyl-pNA and aminoacyl-AMC derivatives in excellent yields starting from either amino acids or their corresponding commercially available N-hydroxysuccinimide esters. The method involved the in situ formation of selenocarboxylate intermediate of protected amino acids and the subsequent non-nucleophilic amidation with an azide. Common protecting groups used in amino acid/peptide chemistry were all well-tolerated. The method was also successfully applied to the synthesis of a dipeptide conjugate, indicating that the methodology is applicable to the synthesis of chromogenic substrates containing short peptides. The method has general applicability to the synthesis of chromogenic and fluorogenic peptide substrates and represents a convenient and high-yield synthesis of N α-protected-aminoacyl-pNAs/AMCs, providing easy access to these important synthons for the construction of chromogenic/fluorogenic protease substrates through fragment condensation or stepwise elongation.
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16

MAES, Marie-Berthe, Anne-Marie LAMBEIR, Kambiz GILANY, Kristel SENTEN, Pieter VAN der VEKEN, Barbara LEITING, Koen AUGUSTYNS, Simon SCHARPÉ, and Ingrid DE MEESTER. "Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)." Biochemical Journal 386, no. 2 (February 22, 2005): 315–24. http://dx.doi.org/10.1042/bj20041156.

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The presence of DPPII (dipeptidyl peptidase II; E.C. 3.4.14.2) has been demonstrated in various mammalian tissues. However, a profound molecular and catalytic characterization, including substrate selectivity, kinetics and pH-dependence, has not been conducted. In the present study, DPPII was purified from human seminal plasma to apparent homogeneity with a high yield (40%) purification scheme, including an inhibitor-based affinity chromatographic step. The inhibitor lysyl-piperidide (Ki~0.9 μM at pH 5.5) was chosen, as it provided a favourable affinity/recovery ratio. The human enzyme appeared as a 120 kDa homodimer. Mass spectrometric analysis after tryptic digestion together with a kinetic comparison indicate strongly its identity with QPP (quiescent cell proline dipeptidase), also called dipeptidyl peptidase 7. pH profiles of both kcat and kcat/Km clearly demonstrated that DPPII/QPP possesses an acidic and not a neutral optimum as was reported for QPP. Kinetic parameters of the human natural DPPII for dipeptide-derived chromogenic [pNA (p-nitroanilide)] and fluorogenic [4Me2NA (4-methoxy-2-naphthylamide)] substrates were determined under different assay conditions. DPPII preferred the chromogenic pNA-derived substrates over the fluorogenic 4Me2NA-derived substrates. Natural human DPPII showed high efficiency towards synthetic substrates containing proline at the P1 position and lysine at P2. The importance of the P1′ group for P2 and P1 selectivity was revealed, explaining many discrepancies in the literature. Furthermore, substrate preferences of human DPPII and dipeptidyl peptidase IV were compared based on their selectivity constants (kcat/Km). Lys-Pro-pNA (kcat/Km 4.1×106 s−1·M−1) and Ala-Pro-pNA (kcat/Km 2.6×106 s−1· M−1) were found to be the most sensitive chromogenic substrates for human DPPII, but were less selective than Lys-Ala-pNA (kcat/Km 0.4×106 s−1·M−1).
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17

Chistov, A. A., A. V. Talanova, M. V. Melnikova, S. S. Kuznetsova, and E. F. Kolesanova. "An Improved Procedure for the Preparation of Thrombin Low Molecular Weight Substrates - Peptide p-Nitroanilides." Biomedical Chemistry: Research and Methods 1, no. 4 (2018): e00057. http://dx.doi.org/10.18097/bmcrm00057.

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Low molecular weight chromogenic thrombin peptide substrates, p-nitroanilides of short peptides protected at their N-terminal amino group, were prepared by solid-phase peptide synthesis on polystyrene-divinylbenzene polymer with trityl groups with preliminary attached p-phenylene diamine moiety. After the cleavage from the resin peptide p-aminoanilides were mildly oxidized to p-nitroanilides with the mixture of potassium sulfate and persulfate. Adsorption onto polymer support Bio-Beads SM-2 with further elution by acetonitrile allowed easy separating peptide p-nitroanilides from the oxidizer and obtaining the thrombin chromogenic substrate preparations with the target substance contents of not less than 95% and yields of 30-40%. Thrombin effectively catalyzed hydrolysis of the prepared substrates with KM and Vmax values of 29-134 mM and 0.03-1/16 mM/s, respectively.
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18

Kasafírek, Evžen, Ladislav Fukal, and Jan Káš. "Chromogenic substrates for papain with a C-terminal S-benzylcysteine residue." Collection of Czechoslovak Chemical Communications 53, no. 12 (1988): 3197–205. http://dx.doi.org/10.1135/cccc19883197.

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Two types of chromogenic substrates for papain were prepared, namely p-nitroanilides of N-acetyltripeptides of general formula Ac-Leu-Leu-A-NAn, where A = Gly, Ala, Leu, and p-nitroanilides of 3-carboxypropionyldi- and tripeptides of general formula Suc-B-Cys(Bzl)-NAn, where B = Gly, Gly-Gly, Ala, Ala-Ala, Leu, Leu-Leu, Gly-Leu, Leu-Ala and Ala-Met. The values of Km, kcat and C (kcat/Km) for these substrates were determined. Suc-Leu-Leu-Cys(Bzl)-NAn is the best substrate for papain its C being 60 000 mol-1 l s-1.
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19

Yeoh, H. H., F. M. Wong, and G. Lim. "Screening for Fungal Lipase Using Chromogenic Lipid Substrates." Mycologia 78, no. 2 (March 1986): 298. http://dx.doi.org/10.2307/3793178.

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20

Richards, A. D., L. H. Phylip, W. G. Farmerie, P. E. Scarborough, A. Alvarez, B. M. Dunn, P. H. Hirel, J. Konvalinka, P. Strop, and L. Pavlickova. "Sensitive, soluble chromogenic substrates for HIV-1 proteinase." Journal of Biological Chemistry 265, no. 14 (June 1990): 7733–36. http://dx.doi.org/10.1016/s0021-9258(19)38989-6.

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21

Manafi, M., W. Kneifel, and S. Bascomb. "Fluorogenic and chromogenic substrates used in bacterial diagnostics." Microbiological Reviews 55, no. 3 (1991): 335–48. http://dx.doi.org/10.1128/mmbr.55.3.335-348.1991.

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22

Manafi, M., W. Kneifel, and S. Bascomb. "Fluorogenic and chromogenic substrates used in bacterial diagnostics." Microbiological Reviews 55, no. 3 (1991): 335–48. http://dx.doi.org/10.1128/mr.55.3.335-348.1991.

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23

Yeoh, H. H., F. M. Wong, and G. Lim. "Screening for Fungal Lipase Using Chromogenic Lipid Substrates." Mycologia 78, no. 2 (March 1986): 298–300. http://dx.doi.org/10.1080/00275514.1986.12025245.

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24

Kolde, H.-J., R. Eberle, H. Hebert, and N. Heimburger. "New Chromogenic Substrates for Thrombin with Increased Specificity." Thrombosis and Haemostasis 56, no. 02 (1986): 155–59. http://dx.doi.org/10.1055/s-0038-1661631.

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SummaryChromogenic substrates for thrombin with high specificity are necessary for several functional assays, especially for the performance of photometric PT and APTT. A new approach to improve the specificity of chromogenic peptide substrates is made coupling tripeptide sequences selective for thrombin to derivatives of 5-amino-2-nitro benzoic acid (ANBA). Especially when the chromophore’s side chain is substituted by amines or amino acids hydrolysis rates by other enzymes like kallikrein, plasmin or factor Xa are decreased significantly compared to corresponding para-nitroanilides of the same amino acid sequence. On the other hand, most of these compounds are still sensitive thrombin substrates. KM-values for thrombin and other enzymes are in the same order of magnitude as corresponding pNA-peptides. ANBA peptide substrates may be useful to measure thrombin selectively in a mixture of other proteases like plasmin, factor Xa or kallikrein and for the colorimetric determination of PT and APTT.
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25

Iida, Hiroshi, Michio Takeuchi, and Eiji Ichishima. "Action ofAspergillusSerine Proteinase on Fluorogenic and Chromogenic Substrates." Agricultural and Biological Chemistry 52, no. 5 (May 1988): 1281–82. http://dx.doi.org/10.1080/00021369.1988.10868820.

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26

SASAMOTO, Kazumi, Mikihiko SAITO, and Yosuke OHKURA. "New chromogenic substrates for N-acetyl-.BETA.-d-glucosaminidase." Analytical Sciences 6, no. 1 (1990): 145–48. http://dx.doi.org/10.2116/analsci.6.145.

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27

Dealler, S. F. "Chromogenic and fluorogenic indicators and substrates in diagnostic microbiology." Reviews in Medical Microbiology 4, no. 4 (October 1993): 198–206. http://dx.doi.org/10.1097/00013542-199310000-00003.

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28

Petrescu, Anca Daniela, H. D. Schell, Gabriela Negroiu, and Maria Caloianu Iordachel. "New Chromogenic Substrates for Rapid Determination of Collagenase Activity." Analytical Letters 23, no. 6 (June 1990): 1039–55. http://dx.doi.org/10.1080/00032719008053444.

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29

Kolde, H. J. "Polyethylene glycol can be validly omitted from chromogenic peptide substrate assay for antithrombin III." Clinical Chemistry 32, no. 8 (August 1, 1986): 1554–56. http://dx.doi.org/10.1093/clinchem/32.8.1554.

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Abstract To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants. Neither the reliability of the calibration curve nor the data for precision and assay kinetics were amended by the addition of either PEG to the (human) thrombin reagent or Tween-80 to the chromogenic substrate. In the same test system, assays with some other chromogenic substrates and with bovine thrombin showed comparable behavior. Evidently, if one follows the working scheme proposed for this kit, the use of surfactants is not warranted.
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30

Krarup, Thomas, Lauritz W. Olson, and Hans Peter Heldt-Hansen. "Some characteristics of extracellular proteases produced by members of the Chytridiales and the Spizellomycetales (Chytridiomycetes)." Canadian Journal of Microbiology 40, no. 2 (February 1, 1994): 106–12. http://dx.doi.org/10.1139/m94-017.

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The extracellular proteolytic enzymes of eight saprophytic, eucarpic, and monocentric isolates from two genera of the order Spizellomycetales and from one genus of the order Chytridiales (Chytridiomycetes) have been partially characterized. The isolectric points of the proteases were estimated from zymograms and demonstrate the existence of three types of proteolytic activity in most isolates. The proteases were tested against synthetic chromogenic peptide substrates and a selection of cations and more complex compounds, and the results suggest that parts of the extracellular proteolytic activities are due to proteases from two groups: the Ca2+ stabilized proteases and the alkaline serine proteases.Key words: serine proteases, metalloproteases, Chytridiomycetes, isoelectric focusing, chromogenic peptide substrates.
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31

Jiang, Yao, Zongzhao Sun, Liyan Zhang, Yuchun Qiao, Fengjuan Liu, Yuanyuan Cai, Wenwen Zhang, Qianqian Zhang, Zhiqiang Duan, and Hua Wang. "Encapsulating chromogenic reaction substrates with porous hydrogel scaffolds onto arrayed capillary tubes toward a visual and high-throughput colorimetric strategy for rapid occult blood tests." Journal of Materials Chemistry B 5, no. 6 (2017): 1159–65. http://dx.doi.org/10.1039/c6tb02836e.

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32

Derman, D. P., A. Green, T. H. Bothwell, B. Graham, L. McNamara, A. P. MacPhail, and R. D. Baynes. "A Systematic Evaluation of Bathophenanthroline, Ferrozine and Ferene in an ICSH-Based Method for the Measurement of Serum Iron." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 26, no. 2 (March 1989): 144–47. http://dx.doi.org/10.1177/000456328902600209.

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The chromogenic substrates ferrozine and ferene were compared to bathophenanthroline disulphonic acid for the measurement of iron concentrations in aqueous and serum samples in an assay based on that of the Iron Panel of the International Committee for Standardisation in Haematology. Ferrozine and ferene were more sensitive than bathophenanthroline. Copper at physiological concentrations in plasma caused only minimal positive interference with all three chromogenic substrates when thioglycollic acid was used as the reducing agent, but when ascorbic acid was used significant positive interference occurred with ferrozine and ferene. Interference due to contaminating haem was comparable with all agents. Bilirubin and carotene produced no interference. Profound reductions in colour development were noted with EDTA plasma.
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33

IIDA, Hiroshi, Michio TAKEUCHI, and Eiji ICHISHIMA. "Action of Aspergillus serine proteinase on fluorogenic and chromogenic substrates." Agricultural and Biological Chemistry 52, no. 5 (1988): 1281–82. http://dx.doi.org/10.1271/bbb1961.52.1281.

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34

Nowak, G., and M. Lopez. "Chromogenic substrates as fundamental tool to design new thrombin inhibitors." Hämostaseologie 25, no. 03 (2005): 267–71. http://dx.doi.org/10.1055/s-0037-1619660.

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SummaryThe structure-activity relationship of dipetalogastin II, the strongest thrombin inhibitor isolated and cloned from the bug Dipetalogaster maximus, was examined by introducing gradual changes into the molecule by means of molecular biological methods. The effect upon its inhibition equilibrium constant was determined after each change by a chromogenic assay. This structural information was fundamental to design new dipetalogastin II-derived inhibitors.Our results suggested that the acidic sequence DEHDHDFEDT corresponding to amino acid residues 49 to 58 of dipetalogastin II reacts with the anion binding exosite (ABE) 1 of thrombin. Based on this finding, we constructed a chimeric molecule consisting of the active site blocking segment of dipetalogastin II (amino acid residues 1 to 48) and the ABE 1 blocking segment of hirudin. This construct showed better thrombin inhibitory activity than both separated segments only after the introduction of a glycine linker between both blocking segments. We thus obtained a thrombin inhibitor called dipetarudin with an inhibition equilibrium constant comparable to that of dipetalogastin II and a molecular mass below that of dipetalogastin.
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35

Petersen, Kenneth Heesche, Jesper Lohse, and Lasse Ramsgaard. "Automated sequential chromogenic IHC double staining with two HRP substrates." PLOS ONE 13, no. 11 (November 20, 2018): e0207867. http://dx.doi.org/10.1371/journal.pone.0207867.

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36

Milgotina, E. I., A. S. Shcheglov, G. B. Lapa, G. G. Chestukhina, and T. L. Voyushina. "Enzymatic synthesis of chromogenic substrates for Glu,Asp-specific proteinases." Journal of Peptide Research 58, no. 1 (July 2001): 12–16. http://dx.doi.org/10.1034/j.1399-3011.2001.00862.x.

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37

Browne, N. K., Z. Huang, M. Dockrell, P. Hashmi, and R. G. Price. "Evaluation of new chromogenic substrates for the detection of coliforms." Journal of Applied Microbiology 108, no. 5 (May 2010): 1828–38. http://dx.doi.org/10.1111/j.1365-2672.2009.04588.x.

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38

Torpenholt, Søs, Jérôme Le Nours, Ulla Christensen, Michael Jahn, Stephen Withers, Peter Rahbek Østergaard, Torben V. Borchert, Jens-Christian Poulsen, and Leila Lo Leggio. "Activity of three β-1,4-galactanases on small chromogenic substrates." Carbohydrate Research 346, no. 13 (September 2011): 2028–33. http://dx.doi.org/10.1016/j.carres.2011.05.017.

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39

Widström, Olle, Joanna Chmielewska, and Margareta Blombäck. "Measurements of enzymatic activities in pleural exudates with chromogenic substrates." Thrombosis Research 42, no. 6 (June 1986): 859–64. http://dx.doi.org/10.1016/0049-3848(86)90123-4.

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40

Migliore, Julia R., and Douglas D. Root. "Using Enzyme-Linked Markers with Chromogenic Substrates in Expansion Microscopy." Biophysical Journal 120, no. 3 (February 2021): 360a. http://dx.doi.org/10.1016/j.bpj.2020.11.2224.

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41

Adam, M., C. Damblon, B. Plaitin, L. Christiaens, and J. M. Frère. "Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive dd-peptidases." Biochemical Journal 270, no. 2 (September 1, 1990): 525–29. http://dx.doi.org/10.1042/bj2700525.

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Various ester and thioester derivatives of hippuric acid have been prepared which were substrates of both beta-lactamases and DD-peptidases. The thioesters were more rapidly hydrolysed by nearly all the enzymes. Surprisingly, the enzymes acted rather efficiently on substrates which did not contain any chiral centre.
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42

Kasafírek, Evžen, Přemysl Frič, and Jan Slabý. "Role of amino acid residues in chromogenic substrates cleaved by pancreatic elastase." Collection of Czechoslovak Chemical Communications 52, no. 6 (1987): 1625–33. http://dx.doi.org/10.1135/cccc19871625.

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Anionic chromogenic substrates, 3-carboxypropionyl tripeptide p-nitroanilides modified with glycine, β-alanine, alanine, leucine and proline in positions P1, P2, and P3 were synthesized. The substrates were digested with pancreatic elastase and the values of Km, kcat, and kcat/Km were determined. Alanine plays a decisive role in position P1, substrates with glycine or β-alanine in this position are not cleaved. The substitution in P2 is dominant for proline; next follow alanine, leucine, and glycine. The substitution in P3 is the least specific one.
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43

Sonder, S. A., and J. W. Fenton. "Thrombin specificity with tripeptide chromogenic substrates: comparison of human and bovine thrombins with and without fibrinogen clotting activities." Clinical Chemistry 32, no. 6 (June 1, 1986): 934–37. http://dx.doi.org/10.1093/clinchem/32.6.934.

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Abstract To assess the thrombin specificity of tripeptide chromogenic substrates, we determined the Michaelis--Menten (Km), catalytic (kcat), and specificity (kcat/Km) constants for S-2238 (H-D-Phe-Pip-Arg-p-nitroanilide), Chromozym-TH (Tos-Gly-Pro-Arg-p-nitroanilide), and Spectrozyme-TH (H-D-hexahydrotyrosyl-Ala-Arg-p-nitroanilide) with high-purity thrombin preparations. Human and bovine alpha-thrombins, prepared by essentially the same procedure, were each greater than 95% in the form of the enzyme (alpha-thrombin) and had a specific fibrinogen-clotting activity greater than 2000 kilo-clotting units per gram of protein (kcu/g). In contrast, human gamma- and bovine beta-thrombins, made by controlled passage of alpha-thrombin through trypsin agarose, were greater than 98% of their respective forms and had fibrinogen-clotting activity less than 1 kcu/g. With the tripeptide chromogenic substrates these four thrombin forms at pH 7.8 and 23 degrees C had Km values of 1.6 to 16 mol/L, kcat values of 35 to 130 s-1, and kcat/Km ratios of 4.7 to 52 L X mol-1 X s-1. Although Km for an individual substrate was slightly higher for bovine than for human alpha-thrombins and although Km values for the nonclotting forms (human gamma- and bovine beta-thrombins) were higher than for clotting forms (alpha-thrombins), we found no major differences among the kinetic values for the three substrates.
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44

Koller, Ernst, and Otto S. Wolfbeis. "Continuous kinetic assay of arylsulfatases with new chromogenic and fluorogenic substrates." Analytica Chimica Acta 170 (1985): 73–80. http://dx.doi.org/10.1016/s0003-2670(00)81727-4.

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45

Farkas, Erzsébet, Lóránt Jánossy, János Harangi, Lili Kandra, and András Lipták. "Synthesis of chromogenic substrates of α-amylases on a cyclodextrin basis." Carbohydrate Research 303, no. 4 (October 1997): 407–15. http://dx.doi.org/10.1016/s0008-6215(97)00187-0.

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46

Miles, R. J., E. L. T. Siu, C. Carrington, A. C. Richardson, B. V. Smith, and R. G. Price. "The detection of lipase activity in bacteria using novel chromogenic substrates." FEMS Microbiology Letters 90, no. 3 (January 1992): 283–87. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05167.x.

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47

Adcock, Philip W., and Christopher P. Saint. "Rapid Confirmation of Clostridium perfringens by Using Chromogenic and Fluorogenic Substrates." Applied and Environmental Microbiology 67, no. 9 (September 1, 2001): 4382–84. http://dx.doi.org/10.1128/aem.67.9.4382-4384.2001.

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ABSTRACT The use of 4-methylumbelliferyl phosphate (MUP) andortho-nitrophenyl-β-d-galactopyranoside (ONPG) for the identification of Clostridium perfringenswas investigated. A liquid assay containing both MUP and ONPG was a highly specific alternative method for C. perfringensconfirmation, reducing incubation time from 48 to only 4 h. The assay solution is easy to prepare, does not require anaerobic conditions for use, and has an extended shelf life.
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48

Zaytsev, Andrey V., Rosaleen J. Anderson, Alexandre Bedernjak, Paul W. Groundwater, Yongxue Huang, John D. Perry, Sylvain Orenga, Celine Roger-Dalbert, and Arthur James. "Synthesis and testing of chromogenic phenoxazinone substrates for β-alanyl aminopeptidase." Organic & Biomolecular Chemistry 6, no. 4 (2008): 682. http://dx.doi.org/10.1039/b716978g.

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49

Kunert, J., and E. Kasafírek. "Preliminary characterization of extracellular proteolytic enzymes of dermatophytes by chromogenic substrates." Medical Mycology 26, no. 3 (January 1988): 187–94. http://dx.doi.org/10.1080/02681218880000261.

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50

Manafi, M. "Fluorogenic and chromogenic enzyme substrates in culture media and identification tests." International Journal of Food Microbiology 31, no. 1-3 (August 1996): 45–58. http://dx.doi.org/10.1016/0168-1605(96)00963-4.

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