Partial characterization of a 36-kDa protein from Clostridium botulinum type E that inhibits trypsin and chymotrypsin

Sakthivel Prabakaran; Bibhuti R. DasGupta

doi:10.2323/jgam.45.163

The Journal of General and Applied Microbiology

Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260

Partial characterization of a 36-kDa protein from Clostridium botulinum type E that inhibits trypsin and chymotrypsin

Sakthivel Prabakaran, Bibhuti R. DasGupta

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Keywords: Clostridium botulinum, partial amino acid sequence, purification, trypsin inhibitor

JOURNAL FREE ACCESS

1999 Volume 45 Issue 4 Pages 163-168

DOI https://doi.org/10.2323/jgam.45.163

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Abstract

A 36-kDa trypsin inhibitor was purified from Clostridium botulinum type E culture supernatant by multiple molecular sieve and ion exchange chromatographic steps. The sequence of the amino-terminal 13 amino acid residues of this single-chain protein is Asn.Gln.Glu.Val.Phe.Asn.Met.Pro.Lys.Phe.Ser.Thr.Ala—. This novel protein that also inhibits chymotrypsin is produced by an organism that does not appear to produce any protease.

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