Separation of Phospholipase A2 in Habu Snake Venom by Glycyrrhizin (GL)-Affinity Column Chromatography and Identification of a GL-Sensitive Enzyme

By means of glycyrrhizin (GL)-affinity and Mono S column chromatographies (HPLC), at least four GL-binding proteins (p25, p17, p15-1 and p15-2) in the two Superdex fractions (P-II and P-III fractions) from Habu snake venom were selectively purified. By determination of their N-terminal partial amino...

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Bibliographic Details
Published in:Biological & pharmaceutical bulletin 1998/06/15, Vol.21(6), pp.574-578
Main Authors: OHTSUKI, Kenzo, ABE, Yoshinori, SHIMOYAMA, Yoshihito, FURUYA, Teisuke, MUNAKATA, Hiroshi, TAKASAKI, Chikahisa
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animal poisons toxicology. Antivenoms
Animals
Biological and medical sciences
Carrier Proteins - chemistry
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Casein Kinase II
Chromatography, Affinity
Crotalid Venoms - chemistry
Crotalid Venoms - enzymology
Glycyrrhizic Acid - metabolism
glycyrrhizin
Group V Phospholipases A2
Habu snake venom
Medical sciences
Molecular Sequence Data
phospholipase A2
Phospholipases A - antagonists & inhibitors
Phospholipases A - chemistry
Phospholipases A - isolation & purification
Phospholipases A - metabolism
Phospholipases A2
Phosphorylation
PLA2 inhibitor
Protein-Serine-Threonine Kinases - metabolism
Toxicology
Trimeresurus - metabolism
Viper Venoms
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Summary:By means of glycyrrhizin (GL)-affinity and Mono S column chromatographies (HPLC), at least four GL-binding proteins (p25, p17, p15-1 and p15-2) in the two Superdex fractions (P-II and P-III fractions) from Habu snake venom were selectively purified. By determination of their N-terminal partial amino acid sequences, a metalloprotease (p25) and three GL-binding phospholipases A2 (gbPLA2s) [PA2Y (p17), PA21 (p15-1) and PA2B (p15-2)] were identified. PA2B (lysine-49 PLA2) was found to be the most sensitive to GL because (i) it strongly bound to a GL-affinity column; and (ii) its enzyme activity was selectively inhibited by low dose (ID50=approx. 1.5μM) of GL, but not by GA. Furthermore, these three gbPLA2s were phosphorylated by casein kinase II (CK-II) in vitro and GL inhibited the CK-II-mediated stimulation of their enzyme activities in vitro.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.21.574