Effect of thyroxine on aspartate aminotransferase and malate dehydrogenase activity in heart muscle of guinea pigs

1970 ◽  
Vol 70 (5) ◽  
pp. 1280-1281
Author(s):  
A. M. Kryshkova ◽  
I. P. Mitev ◽  
A. M. Angelov
Keyword(s):  
Dehydrogenase Activity ◽  
Malate Dehydrogenase ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Guinea Pigs

scholarly journals Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction.

1988 ◽  
Vol 263 (22) ◽  
pp. 10687-10697 ◽  
Author(s):  
L A Fahien ◽  
E H Kmiotek ◽  
M J MacDonald ◽  
B Fibich ◽  
M Mandic
Keyword(s):  
Dehydrogenase Activity ◽  
Malate Dehydrogenase

Production and certification of secondary enzyme reference materials (ERMs). Part 1: Preparation of the sera and some of their properties.

1986 ◽  
Vol 32 (10) ◽  
pp. 1901-1905 ◽  
Author(s):  
J C Koedam ◽  
G M Steentjes ◽  
S Buitenhuis ◽  
E Schmidt ◽  
R Klauke
Keyword(s):  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Reference Material ◽  
Human Serum ◽  
Dehydrogenase Activity ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Glutamate Dehydrogenase Activity ◽  
The Stability ◽  
Clinical Enzymology

Abstract We produced three batches of a human-serum-based enzyme reference material (ERM) enriched with human aspartate aminotransferase (EC 2.6.1.1), alanine aminotransferase (EC 2.6.1.2), creatine kinase (EC 2.7.3.2), and lactate dehydrogenase (EC 1.1.1.27). The added enzymes were not exhaustively purified; thus the final ERMs contained some enzymes as contaminants, of which only glutamate dehydrogenase activity might interfere. The stability during storage and after reconstitution was good. The commutability of the four enzymes in the three ERM batches was also good, except when German or Scandinavian methods for aminotransferases were involved. The temperature-conversion factors for the ERMs were equivalent to those for patients' sera. Reactivation after reconstitution was complete within 5 min and was independent of the temperature of the reconstitution fluid. We believe that these secondary ERMs will aid in the transfer of accuracy between well-defined reference methods and daily working methods so that clinical enzymology results will become more comparable from laboratory to laboratory.

scholarly journals Efficiency of Oxidative Phosphorylation of Heart Muscle Mitochondria from Digitalized Guinea Pigs

1957 ◽  
Vol 5 (3) ◽  
pp. 226-229 ◽  
Author(s):  
KATHARINE ARMSTRONG PLAUT ◽  
MENARD M. GERTLER ◽  
G. W. E. PLAUT
Keyword(s):  
Oxidative Phosphorylation ◽  
Heart Muscle ◽  
Guinea Pigs ◽  
Muscle Mitochondria

scholarly journals The Dissociation into Subunits of Aspartate Aminotransferase from Pig Heart Muscle

1968 ◽  
Vol 6 (4) ◽  
pp. 507-513 ◽  
Author(s):  
B. E. C. Banks ◽  
S. Doonan ◽  
J. Gauldie ◽  
A. J. Lawrence ◽  
C. A. Vernon
Keyword(s):  
Aspartate Aminotransferase ◽  
Heart Muscle

scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase

1973 ◽  
Vol 133 (4) ◽  
pp. 805-819 ◽  
Author(s):  
Francesco Bossa ◽  
Donatella Barra ◽  
Massimo Carloni ◽  
Paolo Fasella ◽  
Francesca Riva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Science And Technology ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Lending Library

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

Sign in / Sign up

Export Citation Format

Share Document