Regulatory properties of 14-day embryo and adult hen heart AMP-deaminase; the influence of pH on the enzyme activity

1984 ◽  
Vol 40 (3) ◽  
pp. 259-261 ◽  
Author(s):  
K. Kaletha
Keyword(s):  
Enzyme Activity ◽  
Amp Deaminase ◽  
Regulatory Properties ◽  
Influence Of Ph

Genetic and other determinants of AMP deaminase activity in healthy adult skeletal muscle

1998 ◽  
Vol 85 (4) ◽  
pp. 1273-1278 ◽  
Author(s):  
Barbara Norman ◽  
Donna K. Mahnke-Zizelman ◽  
Amy Vallis ◽  
Richard L. Sabina
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Mutant Allele ◽  
Fiber Type ◽  
Type I ◽  
Training Status ◽  
Amp Deaminase ◽  
Normal Allele ◽  
Relative Percentage ◽  
Type I Fibers

AMPD1 genotype, relative fiber type composition, training status, and gender were evaluated as contributing factors to the reported variation in AMP deaminase enzyme activity in healthy skeletal muscle. Multifactorial correlative analyses demonstrate that AMPD1 genotype has the greatest effect on enzyme activity. An AMPD1 mutant allele frequency of 13.7 and a 1.7% incidence of enzyme deficiency was found across 175 healthy subjects. Homozygotes for the AMPD1 normal allele have high enzyme activities, and heterozygotes display intermediate activities. When examined according to genotype, other factors were found to affect variability as follows: AMP deaminase activity in homozygotes for the normal allele exhibits a negative correlation with the relative percentage of type I fibers and training status. Conversely, residual AMP deaminase activity in homozygotes for the mutant allele displays a positive correlation with the relative percentage of type I fibers. Opposing correlations in different homozygous AMPD1 genotypes are likely due to relative fiber-type differences in the expression of AMPD1 and AMPD3 isoforms. Gender also contributes to variation in total skeletal muscle AMP deaminase activity, with normal homozygous and heterozygous women showing only 85–88% of the levels observed in genotype-matched men.

AMP-deaminase from human preterm placenta – Kinetic regulatory properties of enzyme

Placenta ◽  
2011 ◽  
Vol 32 (9) ◽  
pp. 704-707 ◽  
Author(s):  
I. Rybakowska ◽  
A. Świeca ◽  
R. Milczarek ◽  
J. Klimek ◽  
K. Kaletha
Keyword(s):  
Amp Deaminase ◽  
Regulatory Properties

scholarly journals Butyrylcholine Esterase: Influence of pH on Enzyme Activity and Irreversible Denaturation.

1959 ◽  
Vol 13 ◽  
pp. 1255-1256 ◽  
Author(s):  
Edith Heilbronn ◽  
Matti Kreula ◽  
Martti Kiesvaara ◽  
B. Högberg ◽  
P. Kneip ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Irreversible Denaturation ◽  
Influence Of Ph

scholarly journals Developmental forms of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme

1988 ◽  
Vol 249 (1) ◽  
pp. 255-261 ◽  
Author(s):  
K Kaletha ◽  
G Nowak
Keyword(s):  
Skeletal Muscle ◽  
Human Fetus ◽  
Human Skeletal Muscle ◽  
Fetal Tissue ◽  
Amp Deaminase ◽  
Half Saturation Constant ◽  
Substrate Saturation ◽  
Regulatory Ligands ◽  
Regulatory Properties ◽  
Similar Kinetic

AMP deaminase isoforms from human skeletal muscle can be separated chromatographically [Kaletha, Spychała & Nowak (1987) Experientia 43, 440-443]. In adult tissue nearly all the AMP deaminase activity was eluted from phosphocellulose with 0.75 M-KCl (‘adult’ isoform), and the remaining activity could be eluted with 2.0 M-KCl. Conversely, most of the AMP deaminase activity from 11-week-old fetal tissue was eluted from phosphocellulose with 2.0 M-KCl (‘fetal’ isoform). In the present paper the kinetic and regulatory properties of AMP deaminase extracted from 11- and 16-week-old fetal skeletal muscle are reported. The two isoforms from 11-week-old human fetus differed distinctly in these properties. The ‘fetal’ isoform had about 5-fold higher half-saturation constant (S0.5) value than the ‘adult’ form. It was also more sensitive to the influence of some important regulatory ligands (ADP, ATP and Pi), and exhibited a different pH/activity profile. The ‘adult’ isoform of AMP deaminase from fetal muscle and the enzyme from mature muscle possessed similar kinetic and regulatory properties. This isoform seems not to be subject to any major modifications during further ontogenesis. This is not true, however, for the ‘fetal’ isoform. In the muscle of 16-week-old human fetus, the ‘fetal’ isoform showed a peculiar, biphasic, type of substrate-saturation kinetics. This phenomenon may reflect appearance of the next, developmentally programmed, isoform of human skeletal-muscle AMP deaminase.

Effect of AMP-Deaminase 3 Knock-Out in Mice on Enzyme Activity in Heart and Other Organs

2014 ◽  
Vol 33 (4-6) ◽  
pp. 319-322 ◽  
Author(s):  
Iwona Rybakowska ◽  
Pawel Romaszko ◽  
Magdalena Zabielska ◽  
Jacek Turyn ◽  
Krystian Kaletha ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Amp Deaminase ◽  
Knock Out
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