Chemical modification of Lys-6 in Taiwan cobra phospholipase A2 with 4-chloro-3,5-dinitrobenzoate

L. S. Chang, Jan-Jong Hung, S. Lin -r., C. C. Chang

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Phospholipase A2 (PLA2) from Naja naja atra snake venom was modified with 4-chloro-3,5-dinitrobenzoate, and one major carboxydinitrophenylated (CDNP) PLA2 was separated by high performance liquid chromato-graphy. CDNP-PLA2 contained only one CDNP group on Lys-6 and showed a 93% drop in enzymatic activity. However, carboxydinitrophenylation did not significantly affect the secondary structure of the enzyme molecule as revealed by the CD spectra, and Ca2+ binding and antigenicity of CDNP-PLA2 were unaffected. Conversion of nitro groups to amino groups resulted in a partial restoration of enzymatic activity of CDNP-PLA2 to 35% of that of native enzyme. These results suggested that the positively charged side chain of Lys-6 played a role in the enzymatic mechanism of PLA2. However, the partial restoration in PLA2 activity reflects that a distortion of the active conformation arising from incorporation of a bulky CDNP group should occur.

Original languageEnglish
Pages (from-to)1207-1213
Number of pages7
JournalBiochemistry and Molecular Biology International
Volume33
Issue number6
Publication statusPublished - 1994

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Elapidae
Phospholipases A2
Chemical modification
Taiwan
Restoration
Snake Venoms
Enzymes
4-chloro-3,5-dinitrobenzoate
Conformations
Molecules
Liquids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

@article{e2aec78f174a4204aeb6c4e0af4492d7,
title = "Chemical modification of Lys-6 in Taiwan cobra phospholipase A2 with 4-chloro-3,5-dinitrobenzoate",
abstract = "Phospholipase A2 (PLA2) from Naja naja atra snake venom was modified with 4-chloro-3,5-dinitrobenzoate, and one major carboxydinitrophenylated (CDNP) PLA2 was separated by high performance liquid chromato-graphy. CDNP-PLA2 contained only one CDNP group on Lys-6 and showed a 93{\%} drop in enzymatic activity. However, carboxydinitrophenylation did not significantly affect the secondary structure of the enzyme molecule as revealed by the CD spectra, and Ca2+ binding and antigenicity of CDNP-PLA2 were unaffected. Conversion of nitro groups to amino groups resulted in a partial restoration of enzymatic activity of CDNP-PLA2 to 35{\%} of that of native enzyme. These results suggested that the positively charged side chain of Lys-6 played a role in the enzymatic mechanism of PLA2. However, the partial restoration in PLA2 activity reflects that a distortion of the active conformation arising from incorporation of a bulky CDNP group should occur.",
author = "Chang, {L. S.} and Jan-Jong Hung and {Lin -r.}, S. and Chang, {C. C.}",
year = "1994",
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Chemical modification of Lys-6 in Taiwan cobra phospholipase A2 with 4-chloro-3,5-dinitrobenzoate. / Chang, L. S.; Hung, Jan-Jong; Lin -r., S.; Chang, C. C.

In: Biochemistry and Molecular Biology International, Vol. 33, No. 6, 1994, p. 1207-1213.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Chemical modification of Lys-6 in Taiwan cobra phospholipase A2 with 4-chloro-3,5-dinitrobenzoate

AU - Chang, L. S.

AU - Hung, Jan-Jong

AU - Lin -r., S.

AU - Chang, C. C.

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AB - Phospholipase A2 (PLA2) from Naja naja atra snake venom was modified with 4-chloro-3,5-dinitrobenzoate, and one major carboxydinitrophenylated (CDNP) PLA2 was separated by high performance liquid chromato-graphy. CDNP-PLA2 contained only one CDNP group on Lys-6 and showed a 93% drop in enzymatic activity. However, carboxydinitrophenylation did not significantly affect the secondary structure of the enzyme molecule as revealed by the CD spectra, and Ca2+ binding and antigenicity of CDNP-PLA2 were unaffected. Conversion of nitro groups to amino groups resulted in a partial restoration of enzymatic activity of CDNP-PLA2 to 35% of that of native enzyme. These results suggested that the positively charged side chain of Lys-6 played a role in the enzymatic mechanism of PLA2. However, the partial restoration in PLA2 activity reflects that a distortion of the active conformation arising from incorporation of a bulky CDNP group should occur.

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