Use of a dual isotope method to measure the interaction of branched chain amino acids and insulin in the stimulation of skeletal muscle protein synthesis

The extent to which branched-chain amino acids (bcaa) and insulin affect the regulation of in vivo skeletal muscle protein synthesis is controversial. To determine their roles in protein synthesis, a dual isotope method using $\sp{14}$C dansyl chloride was adapted for use with radioactive tyrosine. The primary difficulty in adapting the method was defining the stability of the $\sp3$H-label on the tyrosine molecule and characterizing the dansyl chloride reaction with tyrosine. To mitigate these problems: (1) L- (2,3,5,6-$\sp3$H) tyrosine was used, reducing $\sp3$H loss, (2) an acetonitrile/lithium carbonate solvent system was used to increase the efficiency and reproducibility of dansylated tyrosine recovery. These modifications yielded reproducible measurements of protein synthesis and fractional synthesis rates (%/day) that were comparable to literature values.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Nutritional Sciences

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Wibert, Gregory James

Contributors dc:contributor

• Layman, Donald K.

• Biology, Animal Physiology
• Health Sciences, Nutrition

Statement dc:rights

• Copyright 1992 Wibert, Gregory James

Language dc:language

eng

Identifier

AAI9236622
(UMI)AAI9236622

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19252