Purification and characterization of chymotrypsin-like enzyme from rat plasma

R. Senthil Kumar, T. N. Pattabiraman

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A chymotrypsin-like enzyme was purified from rat plasma, involving ammonium sulfate fractionation and chromatographgy on CM-sephadex and red sepharose. The purified enzyme effectively hydrolysed the ester substrates for chymotrypsin (N-acetyl L-tyrosine ethyl ester and N-acetyl L-tryptophan ethyl ester). The Km values for the two substrates were 2.2×10-3M and 9.0×10-3M respectively. The hydrolytic activity of the enzyme was inhibited by phenylmethyl sulfonyl fluoride and tosylphenylalanine chloromethylketone, suggesting the presence of serine and histidine at the active centre. The enzyme exhibited anionic nature and possessed a high molecular weight (MW 71,000) as observed by gel exclusion chromatography on Sephadex G-200. The enzyme was stable upon exposure to pH 7.0-9.0, but was inactivated upon heat treatment at 60°C for 5 min.

Original languageEnglish
Pages (from-to)152-157
Number of pages6
JournalIndian Journal of Clinical Biochemistry
Issue number2
Publication statusPublished - 01-07-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Clinical Biochemistry


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