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Relevant bibliographies by topics / 37-kDa

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Academic literature on the topic '37-kDa'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "37-kDa"

1

Ferreirós, Carlos, Marı́a Teresa Criado, and José A. Gómez. "The neisserial 37 kDa ferric binding protein (FbpA)." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 123, no. 1 (May 1999): 1–7. http://dx.doi.org/10.1016/s0305-0491(99)00044-9.

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Dias, Bianca Da Costa. "Interactions between PrPc and other ligands with the 37-kDa/67-kDa laminin receptor." Frontiers in Bioscience 15, no. 1 (2010): 1150. http://dx.doi.org/10.2741/3667.

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Morel, Etienne, Thibault Andrieu, Fabrice Casagrande, Sabine Gauczynski, Stefan Weiss, Jacques Grassi, Monique Rousset, Dominique Dormont, and Jean Chambaz. "Bovine Prion Is Endocytosed by Human Enterocytes via the 37 kDa/67 kDa Laminin Receptor." American Journal of Pathology 167, no. 4 (October 2005): 1033–42. http://dx.doi.org/10.1016/s0002-9440(10)61192-3.

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Moll, Gert, Emanuele Papini, Raffaele Colonna, Daniela Burroni, John Telford, Rino Rappuoli, and Cesare Montecucco. "Lipid Interaction of the 37-kDa and 58-kDa Fragments of the Helicobacter Pylori Cytotoxin." European Journal of Biochemistry 234, no. 3 (December 1995): 947–52. http://dx.doi.org/10.1111/j.1432-1033.1995.947_a.x.

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Omar, Aadilah, Katarina Jovanovic, Bianca Da Costa Dias, Danielle Gonsalves, Kiashanee Moodley, Robert Caveney, Vusi Mbazima, and Stefan FT Weiss. "Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor." Expert Opinion on Therapeutic Patents 21, no. 1 (November 27, 2010): 35–53. http://dx.doi.org/10.1517/13543776.2011.539203.

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HENDRIKS, L. Wendy, C. Leonie Van VARK, Kees SCHOONDERWOERD, Hans JANSEN, and M. Louis HAVEKES. "Not the mature 56 kDa lipoprotein lipase protein but a 37 kDa protein co-purifying with the lipase mediates the binding of low density lipoproteins to J774 macrophages." Biochemical Journal 330, no. 2 (March 1, 1998): 765–69. http://dx.doi.org/10.1042/bj3300765.

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Lipoprotein lipase (LPL) purified from bovine milk showed variable abilities to stimulate the binding of low density lipoprotein (LDL) to J774 macrophages. The presence of a 37 kDa protein in the LPL sample seemed to be of importance for its stimulatory capacity. In order to investigate this, we isolated LPL from bovine milk via heparin Sepharose chromatography using a continuous salt gradient. Fractions containing the 37 kDa protein (as shown by SDS/PAGE under reducing conditions) eluted first from the column, followed by the 56 kDa LPL protein. The LPL enzymatic activity co-eluted with the 56 kDa protein, whereas the amount of 37 kDa protein fully paralleled the stimulatory effect on the binding of LDL to J774 cells. Samples not containing the 37 kDa protein were far less effective in stimulating the binding. Western blotting using a monoclonal antibody 5D2 against amino acids 396-405 in the carboxy-terminal domain of LPL, showed that the 37 kDa protein may be the C-terminal domain of LPL, presumably generated by proteolytic degradation of the mature LPL protein by milk proteases during its isolation. Furthermore, the functional mass of LPL for stimulation of the binding of LDL, as determined by radiation inactivation, was shown to be 30.9±1.8 kDa. We therefore suggest that cleavage of LPL at protease-sensitive sites causes a conformational change, generating an LPL protein which is more effective in mediating the binding and uptake of lipoproteins by cells.

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Ichihara-Tanaka, K., K. Titani, and K. Sekiguchi. "Role of the carboxyl-terminal Fib2 domain in fibronectin matrix assembly." Journal of Cell Science 108, no. 3 (March 1, 1995): 907–15. http://dx.doi.org/10.1242/jcs.108.3.907.

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A truncated form of fibronectin consisting of the N-terminal 70 kDa and C-terminal 37 kDa regions, designated r70F2, retained the ability to assemble into the extracellular matrix when expressed in cultured fibroblasts (Ichihara-Tanaka et al. (1992) FEBS Lett. 299, 155–158). To elucidate the role of the C-terminal 37 kDa region in fibronectin matrix assembly, we expressed a panel of mutant forms of r70F2 with various deletions and amino acid substitutions in mouse L cells. Although substitution of Ser for two Cys residues in the C-terminal dimerforming segment led to a marked reduction in the matrix assembly activity of r70F2, the resulting monomeric r70F2 still retained a low, but significant activity to assemble into the matrix. Neither the N-terminal 70 kDa nor the C-terminal 37 kDa regions, when expressed as monomeric forms, exhibited any residual activity, suggesting that the core domain of the 37 kDa region consisting of III15 and I10 through I12 modules, termed Fib2 domain, is actively involved in the matrix assembly of r70F2. In support of the role of Fib2 domain, the proteolytic fragment derived from the 37 kDa region inhibited the assembly of r70F2. Furthermore, en bloc deletion of the Fib2 domain or deletion of the I10 through I12 modules from r70F2 resulted in a marked decrease of the matrix assembly activity.(ABSTRACT TRUNCATED AT 250 WORDS)

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Hundt, C. "Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor." EMBO Journal 20, no. 21 (November 1, 2001): 5876–86. http://dx.doi.org/10.1093/emboj/20.21.5876.

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Grosenbach, Douglas W., David O. Ulaeto, and Dennis E. Hruby. "Palmitylation of the Vaccinia Virus 37-kDa Major Envelope Antigen." Journal of Biological Chemistry 272, no. 3 (January 17, 1997): 1956–64. http://dx.doi.org/10.1074/jbc.272.3.1956.

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Speir, J. Paul, Michael W. Senko, Daniel P. Little, Joseph A. Loo, and Fred W. McLafferty. "High-resolution tandem mass spectra of 37-67 kDa proteins." Journal of Mass Spectrometry 30, no. 1 (January 1995): 39–42. http://dx.doi.org/10.1002/jms.1190300108.

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Dissertations / Theses on the topic "37-kDa"

1

Rey, Clémence. "Single chain antibodies against the 37 kDa/67 kDa laminin receptor as tools for prion diseases therapy." Diss., lmu, 2006. http://nbn-resolving.de/urn:nbn:de:bvb:19-48326.

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Leucht, Christoph. "The role of the 37-kDa/67-kDa laminin receptor in the cellular metabolism of the prion protein." Diss., lmu, 2003. http://nbn-resolving.de/urn:nbn:de:bvb:19-8831.

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Gauczynski, Sabine. "Characterization of the 37-kDa/67-kDa laminin receptor as the cell surface receptor for the cellular prion protein." Diss., lmu, 2002. http://nbn-resolving.de/urn:nbn:de:bvb:19-2245.

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Zuber, Chantal. "Antibodies directed against the 37 kDa/67 kDa laminin receptor as therapeutic tools for the treatment of prion diseases and cancer." Diss., lmu, 2008. http://nbn-resolving.de/urn:nbn:de:bvb:19-88001.

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Abouseada, Noha Mohamed. "Role of 37/67-kDa laminin receptor in binding of bacteria causing meningitis." Thesis, University of Nottingham, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.522997.

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Rey, Clémence [Verfasser]. "Single chain antibodies against the 37 kDa, 67 kDa laminin receptor as tools for prion diseases therapy / Clémence Rey." 2005. http://d-nb.info/97908461X/34.

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Leucht, Christoph [Verfasser]. "The role of the 37-kDa, 67-kDa laminin receptor in the cellular metabolism of the prion protein / Christoph Leucht." 2003. http://d-nb.info/967303648/34.

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Gauczynski, Sabine [Verfasser]. "Characterization of the 37-kDa/67-kDa laminin receptor as the cell surface receptor for the cellular prion protein / Sabine Gauczynski." 2002. http://d-nb.info/964632977/34.

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Zuber, Chantal [Verfasser]. "Antibodies directed against the 37 kDa/67 kDa laminin receptor as therapeutic tools for the treatment of prion diseases and cancer / Chantal Zuber." 2008. http://d-nb.info/989934071/34.

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Beck, Julia [Verfasser]. "Genomanalyse beim landwirtschaftlichen Nutztier : Teil 1: Molekularbiologische Analysen zur Vererbung der Leisten- und Hodensackbrüche beim Schwein ; Teil 2: Der 37-kDa-67-kDa Lamininrezeptor (Precursor) im Interspeziesvergleich / vorgelegt von Julia Beck." 2008. http://d-nb.info/989091767/34.

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Book chapters on the topic "37-kDa"

1

Suhadolnik, Robert, Nancy Reichenbach, Camille Martinand-Mari, and Susan Shetzline. "A 37-kDa RNase L." In Chronic Fatigue Syndrome, 55–72. CRC Press, 2002. http://dx.doi.org/10.1201/9781420041002.ch3.

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"A 37-kDa RNase L: A Novel Form of RNase L Associated with Chronic Fatigue Syndrome." In Chronic Fatigue Syndrome, 75–93. CRC Press, 2002. http://dx.doi.org/10.1201/9781420041002-8.

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Revington, M. J., and W. Lee. "Heteronuclear Strategies for the Assignment of Larger protein/DNA complexes: Application to the 37 kDa trp Represser-Operator Complex." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0012.

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The sequence-specific DNA binding function of many proteins is recognized as one of the central mechanisms of regulating transcription and DNA replication and repair. The ability of these proteins to select a short (usually 10 to 20 basepair) sequence out of the entire genome with which to form a stable complex is a prime example of molecular recognition. Atomic resolution structural studies using NMR and X-ray crystallography have emerged as essential techniques in understanding the basis of specificity and stability in these systems. While NMR studies of small DNA-binding domains of proteins have become almost routine (see Kaptein, 1993 for a review) relatively few NMR studies of protein-DNA complexes have been reported. These include the lac repressor headpiece complex (Chuprina et al., 1993). the Antennapedia homeodomain complex (Billetere et al., 1993), the GATA-1 complex (Omichinski et al., 1993). and the Myb DNA binding domain complex (Ogata et al., 1993); all of these complexes are smaller than 20 kDa. In most cases, size limitations have meant that only the DNA binding domain of the protein in complex with a single binding element have been studied. In vivo, however, most DNA binding proteins are much larger than these domains and often function as oligomers. The decrease in quality and increase in complexity of spectra as the molecular weight of the sample increases, limits the number of systems amenable to study using NMR and influences the decision to focus on single domains of multidomain proteins. However, since many DNA-binding proteins are regulated by the binding of ligands, other proteins or phosphorylation, often at sites distal from the DNA-binding domain, it is preferable to study as much of the intact protein as possible in order to characterize allosteric and regulatory mechanisms (Pabo and Sauer, 1992). E. coli trp repressor is a 25 kDa homodimer that regulates operons involved in tryptophan biosynthesis. The dimer is one of the smallest intact proteins that binds sequence specifically to DNA and whose affinity is modulated by an effector (L-tryptophan).

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Conference papers on the topic "37-kDa"

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Morrissey, J. H., D. S. Fair, and T. S. Edgington. "STRUCTURE AND PROPERTIES OF THE HUMAN TISSUE FACTOR APOPROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643738.

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Tissue factor (TF), an integral membrane glycoprotein, is an initiating molecule for the coagulation protease cascade. TF must reside in a phospholipid membrane for optimal activity where it functions as the receptor and essential allosteric activator for factor Vll/VIIa.TF apoprotein was purified from human brain and placenta using factor Vll-affinity chromatography or immunoaffinity chromatography with a mouse anti-TF monoclonal antibody. Both methods resulted in a homogeneous preparation consisting of a highly glycosylated 47 kDa heavy chain and a 12.5 kDa light chain.Removal of asparagine-linked carbohydrate chains with glycopeptidase F reduced the apparentmolecular weight of the heavy chain to 37 kDa but hadno effect on the mobility of the light chain in SDS gel electrophoresis. Electrophoretic analysis of theintact protein with and without reduction indicates that the light chain is disulfide-linked to the heavychain in about half of the TF molecules and is notessential for function.The majority of polyclonal andtwenty- nine monoclonal antibodies against purified TF strongly inhibit coagulation and in all cases aredirected against epitopes on the heavy chain alone. Functional regions of the TF heavy chain have been investigated using a library of twenty-nine monoclonalantibodies and a series of overlapping, synthetic oligopeptides based on sequence information obtained from cloning the cDNA for TF. Supported by NIH grantsHL-16411 and CA-41085.

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Kiso, U., H. Kaudewitz, A. Henschen, B. Åstedt, E. K. O. Kruithof, and F. Bachmann. "DETERMINATION OF INTERMEDIATES, PRODUCTS AND CLEAVAGE SITE IN THE REACTION BETWEEN PLASMINOGEN ACTIVATOR INHIBITOR 2 (PAI 2) AND UROKINASES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642809.

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Several specific inhibitors for both urokinase-type and tissue-type plasminogen activators have in recent years been isolated from various organs and cell lines. The inhibitors isolated from human placenta and from the human histiocytic lymphoma cell line U-937 have been shown to be immunologically related.They are denoted as plasminogen activator inhibitor type 2 (PAI 2). It has earlier been demonstrated by gel electrophoresis that during the inhibition reaction at first complexes are formed between activator and inhibitor and then the inhibitor is cleaved and the complex can be dissociated.In the present study the reactions between urokinase aijd PAI 2 were analysed by means of reversed-phase high-performance liquid chromatography (HPLC) and SDS-polyacrylamide gelelectrophoresis (PAGE). Both high-molecular-weight (54 kDa) and low-molecular weight (33 kDa) urokinase (UK) were used. The PAI 2 was derived from placenta and from U-937 cells. It has a molecular size of L5 kDa. Equimolar amounts of UK and PAI 2 were incubated for 15 min at room temperature. On HPLC and SDS-PAGE analysis new components, corresponding to the UK-PAI 2-complexes, appeared and both UK and PAI 2 disappeared. The apparent sizes of the complexes were approx. 82 kDa and 62 kDa, depending on the type of UK used. The HPLC retention times of the complexes were higher than those of UK or PAI 2. The complexes were stable under the conditions employed for the analyses, but could be completely dissociated by incubation for 1 h at pH 10 and 37°. The released UK behaved identical with the UK starting material. However, the released PAI 2 had decreased in molecular size according to the PAGE analysis, and on HPLC an additional component appeared. As PAI 2 has a blocked N-terminus and the new component shows an N-terminal sequence it must correspond to the C-terminal part of PAI 2. The sequence defines thus the reactive site for the cleavage by the plasminogen activator.

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Goodwin, C. A., M. F. Scully, V. Ellis, and V. V. Kakkar. "THROMBIN BINDING FRAGMENT E GENERATED DURING FIBRINOGENOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642937.

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Binding of fibrinogen by thrombin was measured by inhibition of amidolysis of S2238 and found to be 12 μM. Upon digestion of fibrinogen with plasmin (0.16ugs/mg fibrinogen) for 4 hours at 37°C, thrombin binding activity remained in the supernatants upon heat treatment. The thrombin binding activity in the dialyzed supernatant reached a maximum after two hours coinciding with maximal release of B 1-42 and 45-39 KDa chain fragments. Measured immunologically, levels of fragment E at this time were 45% of the maximum generated after 4 hours digestion. FPA levels in the dialyzed supernatant (measured by RIA and HPLC) after thrombin treatment, were zero and did not increase until 1½ hours after the beginning of digestion, reaching a maximum at 4 hours. The thrombin binding activity generated was stable to further plasmin action. Upon gel chromatography of 2 and 4 hour supernatants, thrombin binding activity coincided closely with fragment E, measured immunologically. Further purification showed the fragment to have Ki for thrombin amidolytic activity of 0.5μM. The fragment also inhibited the thrombin clotting time of plasma but did not affect fibrin monomer polymerization.The fragment was susceptible to very slow inactivation by thrombin but not arvin (though it did inhibit arvin amidolytic activity). A thrombin binding (thrombin inhibitory) fragment is therefore generated during the early stages of f ibrinogenolysis and may be the result of protection by 45 and 39 KDa A α carboxy terminus fragments since E fragments generated in later stages (in the presence of 29 and 25 KDa fragments) do not have this property. These findings may give interesting new insight into thrombin/fibrinogen interaction.

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Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

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We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and non-specific. Stimulation of platelets by thrombin or ADP did not have any effect on the binding of p37 to platelets. The monoclonal antibodies to platelet GP lb (6D1) and GP Ilb-llla (10E5)(A gift of Dr. Barry coller) did not inhibit the binding of p37 to platelets. Fibrinogen (1 mg/ml) and FVIII/vWF (250 ug/ml) reduced the binding slightly. The polyclonal antibodies to p37 as well as concanavalin-A inhibited the binding of p37 to platelets through their direct interaction with p37. Other lectins such as phytohemagglutinin, potato lectin and helix pomatia lectin did not have any effect. At 40 mM, sialic acid, α-D-(+)-glucose, D-(+)-mannose and D-fructose caused 91%,44%,79%, and 63% inhibition of p37 binding respectively. D-(+)-galactose did not interfere with the binding. It is concluded that p37 binds to platelets on the sites other than GP lb and Gp IIb-IIIa and its binding to platelets is inhibited by certain sugars.

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Siddigui, F. A., and E. C. Y. Lian. "PLATELET AGGLUTINATING PROTEIN P37 FROM A THROMBOTIC THROMBOCYTOPENIC PURPURA PLASMA FORMS A COMPLEX WITH IMMUNOGLOBULIN G." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644589.

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A 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura (TTP), has been shown to be present in a subset of TTP patients. The platelet agglutination induced by PAP p37 has been demonstrated to be inhibited by igG from normal adults. To elucidate the mechanism of inhibition of IgG, the interaction between PAP p37 and IgG was studied. The complex formation was demonstrated by the binding of fluid-phase IgG to adsorbed PAP using enzyme-linked immunosorbent assay. The binding was specific, concentration dependent and saturable. The IgG covalently cross-linked to Sepharose 4B bound 125I-PAP but not to 125I-fibrinogen. Sucrose density gradient ultracentrifugation of a mixture of 125I-PAP and IgG also revealed the fluid phase complex formation with a sedimentation value of 19S. Complexes of molecular weight ranging from 180,000 to over 350,000 daltons were also detected by molecular sieve chromatography. The specific complex formation between PAP p37 and IgG is likely to account for the in vitro inhibition of TTP plasma-induced agglutination and , at least partly, the in vivo successful treatment with IgG-containing normal plasma.

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Kitagawa, H., N. Yamamoto, G. Kosaki, and H. Yamazaki. "AN IMPORTANT ROLE OF CARBOHYDRATE MOIETIES ON CANCER CELL MEMBRANE GLYCOPROTEINS IN CANCER CELL-INDUCED PLATELET AGGREGATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644667.

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Platelet aggregation induced by cancer cells may be an essential process in the development of hematogenous metastasis of cancers. A mechanism in HMV-I (human vaginal melanoma cell line)-induced platelet aggregation was studied by using monoclonal antibodies against membrane proteins of cancer cells or platelets. HMV-I cells or their membrana ractions induced platelet aggregation of human heparinized PRP, to which hirudin had no inhibitory effect. The platelet aggregation by HMV-I was completely lost after the pretreatment of the cells with 0.3U/ml neuraminidase for 60 min at 37°C. Preincubation of platelets with monoclonal antibodies against platelet GP lb or GP Ilb/lIIa inhibited HMV-I induced aggregation. A monoclonal antibody MB3 (igM) against another human melanoma (HMMB) which had been transplanted in nude mice was produced by hybridoma technique. Screening studies by cell binding ELISA revealed that MB3 antibody reacted with not only HMMB cells but also many other cells including HMV-I, M7609 (colon carcinoma cell line) and normal fibroblasts. Western-blot analyses showedthat MB3 antibody reacted with multiple, more than ten, proteins with molecular weights ranging from UO to 200 kDa in unreduced SDS-PAGE of HMV-I, HMMB or M7609. In contrast, when .these cells pretreated with neuraminidase were used in Western-blot, MB3 reactivity were all lost. MB3 reacted with at least three glycoproteins of human red cell membrane in Western-blot, but it did not react with human platelets. Immune adherent asgay with trypsin-treated HMV-I or HMMB cells as target cells showed negative reactivity. MB3 antibody inhibited HMV-I-induced aggregation of platelets, but did not inhibit M7609-induced aggregation which depended on thrombin generation.These results suggest that MB3 antibody may be against sialic acid-containing carbohydrate moieties of membrane glycoproteins on these cancercells and that the carbohydrate(s) may play a critical role in' cancer cell-platelet interaction.

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Kempfer, A. C., N. Maugeri, C. Farías, E. Bermejo, M. Gimeno, and M. Lazzari. "PURIFICATION AND PARTIAL CHARACTERIZATION OF A BIOACTIVE SUBSTANCE FROM RAT'S VESSEL WALL INDEPENDENT OF PROSTACYCLIN PRODUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643362.

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Our previous observations provided evidence that a bioactive substance (BAS) with inhibitory effect on platelet aggregation and with inotropic activity on smooth muscle preparations is present in aortic wall of rats treated previously with indomethacin. The ability to inhibit platelet aggregation was used for monitoring its purification and partial characterization. The original sample was extracted by rinsing aortic rings (1.5 mg dried rings) in buffer Krebs (300 μl) for 40 minutes at room temperature. The substance was purified by gel filtration (Bio-gel P-30, Sephadex G-100, Sephadex G-75) and ion exchange chromagra-phy (DEAE cellulose). In the last method, salt gradient elution was performed. Further purification by Sephadex G-50 resulted in removal of 90% of the contaminating substances without a loss of inhibitory activity. The main peak of both chromatographic procedures was analyzed on SDS-PAGE and PAGE with denaturing solvents. The substance was evident by Coomassie Brilliant Blue and periodic acid Schiff staining.In order to determine if the BAS was susceptible to proteolysis, an aliquot of the original sample (29 ug total protein) was incubated with trypsin (final concentration 0.3 μg/ml) and with chymotrypsin (final concentration 3 μg/ml). The BAS activity was not detected. An aliquot of the same original sample was incubated with neuraminidase (final concentration 1.2 units). The BAS activity was detected.The substance appeared to be stable for at least 18 hours at room temperature and 2 hours at 37°C, In addition it was stable over a pH range between 6.8 to 8.6, showing an anionic behaviour.The protein concentration of this substance determined by the method of Lowry was 1 μg/mlPartial characterization supports the conclusion that the substance present in aortic wall of rats is a homogeneous protein, which has a molecular size estimated at 55-65 kDa.

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Veloso, D., M. Shapira, F. Kueppers, and R. W. Colman. "MONOCLONAL ANTIBODY 13G11 RECOGNIZES PREKALLIKREIN, KALLIKREIN AND COMPLEXES OF KALLIKREIN WITH,C1-INHIBITOR AND. α2-MACR0GL0BULIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642901.

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Abnormal prekallikrein (PK) levels in plasma can be due to decreased biosynthesis or increased activation either by surface-activated factor XIIa (e.g., in septicemia) or by other proteases (e.g., in pancreatites). To study the products of activation of PK in plasma, intact normal plasma and plasma exposed to either activating surfaces or factor XII fragment, was immunoblotted from SDS-gels. MAb 13G11 which recognizes purified PK, kallikrein (KAL) and the complexes of KAL with Cl-inhibitor (Cl-Inh) and α2macroglobulin (α2M) formed from purified proteins detected a doubLet (88- and 85-kDa) which comigrated with PK and KAL but was not visible in PK-deficient plasma. Transfer of either PK in normal plasma (25-125 ng) or KAL (50-300 ng) added to PK-deficient plasma was proportional to the amount of protein applied to the SDS-gels. Activation of plasma decreased the intensity of the PK bands with the formation of new bands with molecular weights similar to those of KAL-Cl-Inh and KAL-α2M. Identity was confirmed by MAb 4C3 (reacts with KAL-Cl-In, not with KAL) and a polyclonal antibody to α2M. Increase of incubation temperature from 24 to 37 increased KAL-Cl-Inh and decreased KAL-α2M. Addition of an excess of a2M before surface activation caused an increase of KAL-α2M complex and a decrease of KAL-Cl-Inh. Addition of an excess of Cl-Inh increased KAL-Cl-Inh and decreased KAL-α2M. In addition, activation of Cl-Inh-deficient plasma showed lower KAL-Cl-Inh and higher KAL-a2M than those when normal plasma was activated. When the deficient plasma was treated with CH3NH2 to inactivate α2M, an increase at KAL position was observed since no inhibitors were active. These studies indicate that 13G11 will be useful to detect changes in the distribution of PK, KAL, KAL-Cl-Inh and KAL-α2M associated with abnormal activation of PK and/or abnormal availability of inhibitors in disease.

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