Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An anticoagulant protein, factor IX/factor X-binding protein (IX/X-bp), isolated from the venom of Trimeresurus flavoviridis, binds with factor IX and factor X in the presence of Ca2+ with a 1 to 1 stoichiometry (Atoda, H., and Morita, T. (1989) J. Biochem. (Tokyo) 106, 808-813). Analysis of S-pyridylethylated IX/X-bp by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a 16.0-kDa band (designated the A chain) and a 15.5-kDa band (designated the B chain). These two chains were separated by reversed-phase high performance liquid chromatography, and their complete amino acid sequences were determined by sequencing of the peptides obtained after digestion with lysyl endopeptidase, chymotrypsin, and V8 protease from Staphylococcus aureus and after chemical cleavage with cyanogen bromide. The A chain had an amino-terminal sequence of Asp-Cys-Leu-Ser-Gly- and consisted of 129 residues with Mr 14,830. The B chain has an amino-terminal sequence of Asp-Cys-Pro-Ser-Asp- and consists of 123 residues of Mr 14,440. There was 47% identity between the A and the B chain. The sequence of IX/X-bp showed 25-37% identity with that of the C-type carbohydrate recognition domain-like structure of acorn barnacle lectin, human and rat asialoglycoprotein receptors, the human lymphocyte Fc epsilon receptor for immunoglobulin E, proteoglycan core protein, pancreatic stone protein, and tetranectin. The sequences of the first 18 amino acid residues of both the A and B chains were also, to a certain extent, homologous to the partial amino acid sequence of the b subunit of factor XIII, a member of the beta 2-glycoprotein I-like family. In this region, some similarity with the amino-terminal amino acid sequence of botrocetin was also observed.
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PMID:The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E. 183 Nov 97

Swarm rat chondrosarcoma contains a hyaluronan-binding protein of molecular mass 102 kDa (HABP102). The protein is present in 4 M-guanidinium chloride extracts of the chondrosarcoma and can be incorporated into reconstituted proteoglycan aggregates, but it is not present in native proteoglycan aggregates or in 0.5 M-guanidinium chloride extracts. HABP102 is unlikely to be an integral membrane protein, as it does not require detergent for extraction, is not enriched in hydrophobic amino acids and does not bind avidly to octyl-Sepharose. The protein stains poorly with Coomassie Blue and is only visible on PAGE gels after staining with silver. Disulphide bonds are essential for the binding of HABP102 to hyaluronan, and bivalent cations are not required for this interaction. HABP102 can be purified from dissociative chondrosarcoma extracts by sequential density-gradient centrifugation, hyaluronan-Sepharose affinity chromatography and hydrophobic-interaction chromatography. The amino acid composition is similar to that of domains 1-4 of the chondrosarcoma proteoglycan core protein, but peptide analysis after digestion with Staphylococcus aureus V8 proteinase and chymotrypsin and different immunoreactivity suggest that HABP102 is not closely related to proteoglycan hyaluronan-binding region. HABP102 is a glycoprotein containing N-acetylgalactosamine, N-acetylglucosamine, mannose and galactose.
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PMID:Purification and characterization of a hyaluronan-binding protein from rat chondrosarcoma. 231 94

The ternary complex consisting of a 65-kDa peptide originating from the proteoglycan core protein and a 43-kDa link protein bound to hyaluronic acid was purified from a clostripain digest of the rat chondrosarcoma aggregating proteoglycan and 14C-carbamylated with potassium [14C]cyanate. At a pH of 8.0, 14C-carbamylation of the alpha-NH2 groups in the N-terminal amino acids was favored over carbamylation of epsilon-NH2 groups in the lysinyl residues for both the 65- and 43-kDa species. Two-dimensional tryptic peptide maps revealed a single major, distinctly different, fluorographic spot for each. These tryptic peptides had approximate masses of 4.5 kDa (from the 65-kDa species) and 3.0 kDa (from the 43-kDa species) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels and each contained greater than 60% of the total radioactivity associated with its original polypeptide. Primary amino acid sequencing of the 65-kDa species gave a defined sequence for the first 4 N-terminal residues, whereas sequencing through the first 4 residues of a fully carbamylated species gave no dabsylated derivative for the first residue but identical residues in position 2-4 as for the noncarbamylated species and loss of radioactive derivative. Digests of 14C-carbamylated ternary complex with alpha-chymotrypsin resulted in a limit 14C-carbamylated 55-kDa species which contained greater than 85% of the radiolabel originally in the 65-kDa peptide. Similarly, trypsin generated two radiolabeled species, 60 and 58 kDa. These limit digest peptides (55, 60, 58 kDa) all contained the 4.5-kDa N-terminal tryptic peptide. Thus peptides removed from the 65-kDa peptide digestion with either alpha-chymotrypsin or trypsin were on the carboxyl end of the molecule.
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PMID:N-terminal carbamylation of the hyaluronic acid-binding region and the link protein from the chondrosarcoma proteoglycan aggregate. 353 3