Isolation, purification and partial characterization of a lectin from the seeds of Capiscum annum Linn. cv. California wonder

Date

3-2000

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Marivic S. Lacsamana

Co-adviser

Florinia E. Merca

Abstract

ABSTRACT OROCAY, ANALYN GAGATIGA, Institute of Chemistry, College of Arts and Sciences, University of the Philippines Los Banos, March, 2000. Isolation, Purification, and Partial Characterization of a Lectin from the Seeds of Capsicum annum Linn cv. California Wonder.

Adviser: Dr. Marivic S. Lacsamana

One lectin was isolated from the seeds of Capsicum annum Linn cv. California Wonder by extraction with 0.02 M phosphate buffered saline (p1-1 7.2). The lectin was purified by ammonium sulfitte precipitation, dialysis, isoelectric precipitation, and gel filtration using Sephadex 0-200. Only one band was observed by electrophoresis on polyacrylamide gel under non-denaturing conditions. The blood type and blood group specificity of the lectin was determined by hemagglutination assay using human blood types A, 13, O. and AB and blood from calf and goat. The sugar-binding specificity of the !win was determined using maltose, fructose, fucose, glucose, lactose, mannose, galactose. glucoseamine, N-acetylglucoseamine, rhamnose, sucrose, and xylose as inhibitory sugars. The molecular mass of the purified lectin was estimated using sodium dodccyl sulfate polyacrylamide gel electrophoresis (SUS-PAGE). The lectin was found to be non-blood type and non-blood group specific because it agglutinated the erythrocytes from human blood types A, B, 0, and AB as well as those from goat and calf. Hernagglutination assay of the lectin was not inhibited by all the sugars tested. *I he molecular weight of the purified lectin was estimated to be GO kD by SDS-PAGE.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2000 C4 O76

Document Type

Thesis

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