Primary Structure of an Inactive Mutant of Phospholipase A2 in the Venom of Bungarus fasciatus (Banded krait)1

Autor:	Po-Yao Kuo, Chen-Hsien Chang, Chen-Sheng Liu, Mu-Chin Tzeng, Tung-Bin Lo, Chiu-Chen Tseng, Shun-Wen Chen, Jin-Mei Chen
Rok vydání:	1992
Předmět:	biology Protein primary structure Venom General Medicine Anatomy biology.organism_classification complex mixtures Biochemistry Enzyme assay Bungarus Phospholipase A2 Banded krait Snake venom biology.protein Molecular Biology Peptide sequence
Zdroj:	The Journal of Biochemistry. 112:707-713
ISSN:	1756-2651 0021-924X
DOI:	10.1093/oxfordjournals.jbchem.a123962
Popis:	From the acidic components of Bungarus fasciatus venom, a very small amount (0.16%) of a novel phospholipase A2 was obtained. Both neurotoxicity and enzyme activity were found to be lacking. Amino acid sequence study showed that it has a normal backbone of group I snake venom phospholipase A2 with 118 amino acid residues. The lack of enzyme activity was attributed to its mutation of the indispensable Asp residue to an Ala residue, i.e., the usual His-Asp47 turned out to be His-Ala47. This is the eighth isoform of phospholipase A2 found from the venom of Bungarus fasciatus. Examination of structural homology with three other isoforms revealed 66% similarity at most.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::82ec0cd9a041c5b10910186ce9067cef https://doi.org/10.1093/oxfordjournals.jbchem.a123962 Zobrazit plný text záznamu