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

L. S. Chang, J. J. Hung, S. Lin -r., C. C. Chang

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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
Issue number6
Publication statusPublished - 1994 Jan 1

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Chemical modification of Lys-6 in Taiwan cobra phospholipase A2 with 4-chloro-3,5-dinitrobenzoate'. Together they form a unique fingerprint.

Cite this