Purification and partial characterization of adenylate kinase from germinating mung beans (Vigna radiata)

Date

5-1991

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Dario C. Sabularse

Abstract

Adenylate kinase from mung bean seeds was purified using dye-ligand chromatography system.  Among the sixteen columns screened to determine the best negative-positive dye-ligand system.  the Remazol Hoeacht Violet R. and the Procion Red H-E7B dyes were chosen asa the best negative and positive adsorbents.  respectively.  The purified enzyme from the combination of the negative.  positive.  and Sephadex G-100 column chromatography had a specific activity of 7.32 U/mg protein and is 122-fold pure.  Analysis of the Michaellis-Menten and is 132-fold pure.  Analysis of the Michaelis-Menten constant showed that the enzyme has a higher affinity towards ATP (0.16mM) than AMP (0.64mM).  The optimal pH for  the activity of adenylate kinase was observed at pH 7.5.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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