STRUCTURES AND FUNCTION OF FATTY ACID BINDING PROTEINS FROM RAT HEART AND SKELETAL MUSCLE.
Item
-
Title
-
STRUCTURES AND FUNCTION OF FATTY ACID BINDING PROTEINS FROM RAT HEART AND SKELETAL MUSCLE.
-
Identifier
-
AAI8611379
-
identifier
-
8611379
-
Creator
-
SAID, BOCTOR FAHEEM.
-
Contributor
-
Horst Schulz
-
Date
-
1986
-
Language
-
English
-
Publisher
-
City University of New York.
-
Subject
-
Chemistry, Biochemistry
-
Abstract
-
The low molecular weight fatty acid binding proteins (FABP) present in the cytosols of rat heart, liver and skeletal muscle were studied. The three proteins were purified to apparent homogeneity as judged by polyacrylamide gel electrophoresis. Antibodies to the FABP from rat heart and rat liver were used to study the tissue distributions of the heart and liver proteins. This evaluation suggests rat heart-like FABP to be present in heart, skeletal muscle, kidney and stomach, whereas rat liver FABP was identified only in liver and small intestine. Thus, the heart and liver FABPs are immunologically unrelated.;Although FABPs from rat heart and skeletal muscle are immunologically related and have similar amino acid compositions, they are different proteins as judged by their ultraviolet spectra, their electrophoretic mobilities on polyacrylamide gels in the absence or presence of sodium dodecyl sulfate and by their capacities to bind fatty acids before and after delipidation of the proteins. The presence of two moles of Ca('2+) per mole of skeletal muscle FABP prompted an investigation into the possible identity of this protein with parvalbumin. Based on its Ca('2+) content pI, amino acid composition and ultra-violet spectrum, the FABP of rat skeletal muscle is closely related to or identical with rat parvalbumin.;The possible function of rat heart FABP as a cytosolic carrier of fatty acids was assessed by studying the effect of this protein on the transfer of oleic acid from a donor membrane to liposomes. The rate of oleic acid transfer to liposomes was unaffected by the presence of rat heart FABP.
-
Type
-
dissertation
-
Source
-
PQT Legacy CUNY.xlsx
-
degree
-
Ph.D.
-
Program
-
Biochemistry
