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Title: Purification and characterization of a kinin-releasing and fibrinogen-clotting serine proteinase (KN-BJ) from the venom of Bothrops jararaca, and molecular closing and sequence analysis of its cDNA
Authors: Serrano, SMT
Hagiwara, Y.
Murayama, N.
Higuchi, Z.
Mentele, R.
Sampaio, Claudio Augusto Machado [UNIFESP]
Camargo, Antonio Carlos Martins de [UNIFESP]
Fink, E.
Inst Butantan
Showa Univ
Univ Munich
Universidade Federal de São Paulo (UNIFESP)
Keywords: kinin
Bothrops jararaca
snake venom serine proteinase
Issue Date: 1-Feb-1998
Publisher: Springer
Citation: European Journal of Biochemistry. New York: Springer Verlag, v. 251, n. 3, p. 845-853, 1998.
Abstract: Two forms of a proteinase, KN-BJ 1 and 2, were purified to homogeneity from the venom of Bothrops jararaca. in SDS/PAGE reduced KN-BJ 1 and 2 migrated as single bands with molecular masses of 38 kDa and 39 kDa. the two enzymes have similar N-terminal amino acid sequences and specific activities on synthetic chromogenic substrates, and both release bradykinin fi om bovine low-molecular-mass kininogen. KN-BJ 1 and KN-BJ 2 clot fibrinogen with specific activities of 245 NIH U/mg and 219 NIH U/mg, releasing only fibrinopeptide A. the amidolytic, kinin-releasing and coagulant activities are inhibited by phenylmethylsulfonyl fluoride, demonstrating that KN-BJ is a serine proteinase. Benzamidine derivatives, which are competitive inhibitors of trypsin-like proteinases. also inhibited the amidolytic activity of KN-BJ. A cDNA clone (HS104, 2.2 kb) has been isolated from a cDNA library of B. jararaca venom glands with an ORF of 771 bp. the deduced amino acid sequence contains segments that are identical to the sequences of the N-terminus and three tryptic peptides of KN-BJ 2. Therefore, the cDNA is believed to represent the gene of KN-BJ 2. the deduced amino acid sequence indicates that KN-BJ 2 is synthesized as a prezymogen of 257 amino acids with a putative signal peptide of 18 amino acids and an activating peptide of six amino acid residues. the sequence of 233 amino acids representing the mature enzyme exhibits high similarity to sequences of serine proteinases isolated from crotalid venoms.
ISSN: 0014-2956
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