Carboxyl group reactivity in actin

Conference · Wed Jan 01 00:00:00 EST 1986

OSTI ID:7119773

Elzinga, M

While earlier work showed that the carboxyl groups of proteins could be quantitatively coupled to amino groups at pH 4.75 in the presence of EDC and a denaturing agent, the work presented here indicates that under milder conditions the modification of sidechain carboxyls is limited and somewhat specific. Most of the incorporated glycine ethyl ester (GEE) is apparently bound to five carboxyls. The total GEE incorporated was 3 to 4 moles/mole of protein as measured by an increase in Gly upon acid hydrolysis and amino acid analysis, as well as total radioactivity. 3.55 residues were found in peptides, 2.75 bound to residues 1 to 4, and 0.8 bound to Gly-100. 9 refs., 2 figs., 2 tabs.

• Research Organization: Brookhaven National Lab., Upton, NY (USA)
• DOE Contract Number: AC02-76CH00016
• OSTI ID: 7119773
• Report Number(s): BNL-38848; CONF-8608145-1; ON: DE87003197
• Resource Relation: Conference: 6. international conference on methods in protein sequence analysis, Seattle, WA, USA, 1 Aug 1986; Other Information: Portions of this document are illegible in microfiche products
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ACTIN
ENZYMATIC HYDROLYSIS
AMINO ACID SEQUENCE
CARBON 14 COMPOUNDS
GEL PERMEATION CHROMATOGRAPHY
LIQUID COLUMN CHROMATOGRAPHY
PEPTIDES
STRUCTURE-ACTIVITY RELATIONSHIPS
TRACER TECHNIQUES
CHEMICAL REACTIONS
CHROMATOGRAPHY
DECOMPOSITION
HYDROLYSIS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
LYSIS
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
PROTEINS
SEPARATION PROCESSES
SOLVOLYSIS
550201* - Biochemistry- Tracer Techniques