Abstract

Human placental alkaline phosphatase was purified by butanol extraction, methanol precipitation and chromatography on DEAE-cellulose. The pH optimum was found to be 10.9. The enzyme was competitively inhibited by di-ethyl-p-nitrobenzyl-phosphonate and copper sulfate. An increase in enzymatic activity occurred in the presence of the phosphate ion (HPO4) and ATP.

The enzyme was crystallized from a 40% saturated solution of ammonium sulfate and shown to be homogeneous by sedimentation analysis. Homogeneity of the enzyme was also demonstrated using poly-acrylamide-gel-electrophoresis. At a pH of 7.5% the electrophoretic pattern yielded a single band and showed no significant contamination.

The metabolic transformation of progesterone incubated with preparations of rat adrenal tissues was found to produce the adrenocortical steroid, corticosterone. Corticosterone was isolated from rat adrenals and characterized by its mobility in paper and thin layer chromatography. The migration rates (Rf's) of corticosterone and of its acetylated product were found to be the same as its corresponding steroid standard.

LLU Discipline

Biochemistry

Department

Biochemistry

School

Graduate School

First Advisor

R. Bruce Willcox

Second Advisor

Charles W. Slattery

Degree Name

Master of Arts (MA)

Degree Level

M.A.

Year Degree Awarded

1977

Date (Title Page)

6-1977

Language

English

Library of Congress/MESH Subject Headings

Placental Extracts; Steroids

Type

Thesis

Page Count

xii; 89

Digital Format

PDF

Digital Publisher

Loma Linda University Libraries

Usage Rights

This title appears here courtesy of the author, who has granted Loma Linda University a limited, non-exclusive right to make this publication available to the public. The author retains all other copyrights.

Collection

Loma Linda University Electronic Theses and Dissertations

Collection Website

http://scholarsrepository.llu.edu/etd/

Repository

Loma Linda University. Del E. Webb Memorial Library. University Archives

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