Ecto- and cytosolic 5′-nucleotidases in normal and AMP deaminase-deficient human skeletal muscle

2006 ◽  
Vol 387 (1) ◽  
Author(s):  
Frank Hanisch ◽  
Ylva Hellsten ◽  
Stephan Zierz
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Amp Deaminase

EFFECT OF ENDURANCE TRAINING ON AMP DEAMINASE ACTIVITY IN HUMAN SKELETAL MUSCLE.

1995 ◽  
Vol 27 (Supplement) ◽  
pp. S43 ◽  
Author(s):  
B. Norman ◽  
C-J. Sundberg ◽  
M. Viru ◽  
E. Jansson
Keyword(s):  
Skeletal Muscle ◽  
Endurance Training ◽  
Human Skeletal Muscle ◽  
Amp Deaminase

The influence of phosphate, fluoride and potassium ions on the activity of amp-deaminase from human skeletal muscle

1976 ◽  
Vol 7 (1-2) ◽  
pp. 67-71 ◽  
Author(s):  
Krystian Kaletha ◽  
Andrrzej Stankiewicz ◽  
Wieslaw Makarewicz ◽  
Mariusz Zydowo
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Potassium Ions ◽  
Amp Deaminase

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.

Developmental forms of human skeletal muscle AMP-deaminase

1987 ◽  
Vol 43 (4) ◽  
pp. 440-443 ◽  
Author(s):  
K. Kaletha ◽  
J. Spychala ◽  
G. Nowak
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Amp Deaminase

Immunohistochemical localization of AMP deaminase in rimmed vacuoles in human skeletal muscle

1987 ◽  
Vol 10 (9) ◽  
pp. 790-800 ◽  
Author(s):  
Itsuro Higuchi ◽  
Shoichi Ishiura ◽  
Ikuya Nonaka ◽  
Hideo Sugita
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Immunohistochemical Localization ◽  
Amp Deaminase ◽  
Rimmed Vacuoles
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