A novel plasminogen activator from snake venom, purification, characterization, and molecular clonin

CORC > 昆明动物研究所 > 昆明动物研究所 > 动物模型与人类重大疾病机理重点实验室 > 动物活性蛋白多肽组学

	A novel plasminogen activator from snake venom, purification, characterization, and molecular clonin
	Zhang Y 1,2; Wisner A 1; Xiong YL 2; Bon C.
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	1995
卷号	270 期号:17 页码:10246-10255
英文摘要	A novel plasminogen activator from Trimeresurus stejnegeri venom (TSV-PA) has been identified and purified to homogeneity. It is a single chain glycoprotein with an apparent molecular weight of 33,000 and an isoelectric point of pH 5.2. It specifically activates plasminogen through an enzymatic reaction. The activation of human native GIu-plasminogen by TSV-PA is due to a single cleavage of the molecule at the peptide bond Arg(561)-Val-(562). Purified TSV-PA, which catalyzes the hydrolysis of several tripeptide p-nitroanilide substrates, does not activate nor degrade prothrombin, factor X, or protein C and does not clot fibrinogen nor show fibrino(geno)lytic activity in the absence of plasminogen. The activity of TSV-PA was readily inhibited by phenylmethanesulfonyl fluoride and by p-nitrophenyl-p-guanidinobenzoate. Oligonucleotide primers designed on the basis of the N-terminal and the internal peptide sequences of TSV-PA were used for the amplification of cDNA fragments by polymerase chain reaction. This allowed the cloning of a full-length cDNA encoding TSV-PA from a cDNA library prepared from the venom glands. The deduced complete amino acid sequence of TSV-PA indicates that the mature TSV-PA protein is composed of 234 amino acids and contains a single potential N-gIycosylation site at Asn(1G1). The sequence of TSV-PA exhibits a high degree of sequence identity with other snake venom proteases: 66% with the protein C activator from Aghistrodon contortrix contortrix venom, 63% with batroxobin, and 60% with the factor V activator from Russell's viper venom. On the other hand, TSV-PA shows only 21-23% sequence similarity with the catalytic domains of u-PA and t-PA. Furthermore, TSV-PA lacks the sequence site that has been demonstrated to be responsible for the interaction of t-PA (KHRR) and u-PA (RRHR) with plasminogen activator inhibitor type 1.
收录类别	SCI
语种	英语
公开日期	2013-04-09
内容类型	期刊论文
源URL	[http://159.226.149.42:8088/handle/152453/7323]
专题	昆明动物研究所_动物活性蛋白多肽组学昆明动物研究所_其他
作者单位	1.INST PASTEUR,UNITE VENINS,F-75724 PARIS 15,FRANCE 2.CHINESE ACAD SCI,KUNMING INST ZOOL,KUNMING 650223,PEOPLES R CHINA
推荐引用方式 GB/T 7714	Zhang Y,Wisner A,Xiong YL,et al. A novel plasminogen activator from snake venom, purification, characterization, and molecular clonin[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,1995,270(17):10246-10255.
APA	Zhang Y,Wisner A,Xiong YL,&Bon C..(1995).A novel plasminogen activator from snake venom, purification, characterization, and molecular clonin.JOURNAL OF BIOLOGICAL CHEMISTRY,270(17),10246-10255.
MLA	Zhang Y,et al."A novel plasminogen activator from snake venom, purification, characterization, and molecular clonin".JOURNAL OF BIOLOGICAL CHEMISTRY 270.17(1995):10246-10255.