Purification and Partial Characterization of Trypsin Inhibitor from Watermelon Seeds

Bilbis, L.S; Shehu, R.A; Abubakar, M.K

dc.contributor.author	Bilbis, L.S
dc.contributor.author	Shehu, R.A
dc.contributor.author	Abubakar, M.K
dc.date.accessioned	2017-10-31T10:03:31Z
dc.date.available	2017-10-31T10:03:31Z
dc.date.issued	2001
dc.identifier.issn	0189·4757
dc.identifier.uri	http://hdl.handle.net/123456789/272
dc.description.abstract	Several fractions demonstrating trypsin inhibitory activity were isolated from the seeds of watermelon. One of the mrnbnors was punfied to apparent homogeneity and partially characterized emploYing ion-exchange chromatography on DEAESephadex A-50, gel filtration on Sepnadex G100 and affinity chromatography on Trypsrn-Aqarose. The inhibitor has relative molecular mass of 10,000 by gel filtration. The inhibitor was resistant to heat up to iO"C for 30 minutes and acidic condition down to pH 4.0. Possibly the inhibitor belongs to the famlfy of low molecular weight heat resistant protease inhibitors.	en_US
dc.language.iso	en	en_US
dc.publisher	Nigerian Journal of Biochemistry and Molecular Biology	en_US
dc.subject	Department of Biochemistry	en_US
dc.title	Purification and Partial Characterization of Trypsin Inhibitor from Watermelon Seeds	en_US
dc.type	Article	en_US