scholarly journals Identification of an arginine residue important for catalytic activity in the primary structure of d-glyceraldehyde 3-phosphate dehydrogenase. Studies with the rat skeletal-muscle enzyme

1981 ◽  
Vol 199 (3) ◽  
pp. 757-765 ◽  
Author(s):  
N D Vospelnikova ◽  
M I Safronova ◽  
E R Shuvalova ◽  
L A Baratova ◽  
S P Kniazev ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Catalytic Activity ◽  
Experimental Evidence ◽  
Primary Structure ◽  
Structural Rearrangements ◽  
Rat Skeletal Muscle ◽  
Active Centre ◽  
Muscle Enzyme ◽  
Tryptic Digest ◽  
Arginine Residues

The reaction of holo-(D-glyceraldehyde 3-phosphate dehydrogenase) (EC 1.2.1.12) from rat skeletal muscle with [14C]butanedione in 0.05 M-NH4HCO3, pH 8.0, resulted in modification (*) of two arginine residues per subunit with a concomitant loss of catalytic activity. From a tryptic digest of the modified protein two radiolabelled peptides were isolated, with the following sequences: (1)Val-Ile-Ile-Asn-Ala-Pro-Thr-Ala-Asp-Ala(Glx,Met,Leu,Phe,Met)Gly-Val-Asx-Arg- Glx(His,Tyr)Ser-Lys and (2) Asp-Ala-Gly-Ala-Thr-Ile-Ala-Leu(Asx,Glx,Arg,Phe,Val)Lys. By comparison of the data with the known sequences of homologous enzymes, the localization of the modified residues was established. The first peptide was identified as corresponding to residues 116--139, the second to residues 293--306. Experimental evidence from this and previous studies suggests that arginine-134 is important for the catalytic activity of the rat muscle enzyme, being involved in structural rearrangements accompanying the organization of the active centre on the binding of coenzyme and substrate.

Effect of training on insulin binding to rat skeletal muscle sarcolemmal vesicles

1986 ◽  
Vol 250 (5) ◽  
pp. E570-E575
Author(s):  
G. K. Grimditch ◽  
R. J. Barnard ◽  
S. A. Kaplan ◽  
E. Sternlicht
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Exercise Training ◽  
Insulin Binding ◽  
Whole Body ◽  
Rat Skeletal Muscle ◽  
Binding Studies ◽  
Muscle Enzyme ◽  
Intravenous Glucose ◽  
High Affinity

We examined the hypothesis that the exercise training-induced increase in skeletal muscle insulin sensitivity is mediated by adaptations in insulin binding to sarcolemmal (SL) insulin receptors. Insulin binding studies were performed on rat skeletal muscle SL isolated from control and trained rats. No significant differences were noted between groups in body weight or fat. An intravenous glucose tolerance test showed an increase in whole-body insulin sensitivity with training, and specific D-glucose transport studies on isolated SL vesicles indicated that this was due in part to adaptations in skeletal muscle. Enzyme marker analyses revealed no differences in yield, purity, or contamination of SL membranes between the two groups. Scatchard analyses indicated no significant differences in the number of insulin binding sites per milligram SL protein on the high-affinity (15.0 +/- 4.1 vs. 18.1 +/- 6.4 X 10(9)) or on the low-affinity portions (925 +/- 80 vs. 884 +/- 106 X 10(9)) of the curves. The association constants of the high-affinity (0.764 +/- 0.154 vs. 0.685 +/- 0.264 X 10(9) M-1) and of the low affinity sites (0.0096 +/- 0.0012 vs. 0.0102 +/- 0.0012 X 10(9) M-1) also were similar. These results do not support the hypothesis that the increased sensitivity to insulin after exercise training is due to changes in SL insulin receptor binding.

scholarly journals Primary Structure of Parvalbumin from Rat Skeletal Muscle

1982 ◽  
Vol 127 (2) ◽  
pp. 381-389 ◽  
Author(s):  
Martin W. BERCHTOLD ◽  
Claus W. HEIZMANN ◽  
Kenneth J. WILSON
Keyword(s):  
Skeletal Muscle ◽  
Primary Structure ◽  
Rat Skeletal Muscle

Primary structure and expression of a sodium channel characteristic of denervated and immature rat skeletal muscle

Neuron ◽  
1990 ◽  
Vol 4 (2) ◽  
pp. 233-242 ◽  
Author(s):  
Roland G. Kallen ◽  
Zu-Hang Sheng ◽  
Jane Yang ◽  
Liquiong Chen ◽  
Richard B. Rogart ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sodium Channel ◽  
Primary Structure ◽  
Rat Skeletal Muscle ◽  
Immature Rat ◽  
Channel Characteristic

scholarly journals Functional arginine residues of D-glyceraldehyde-3-phosphate dehydrogenase from rat skeletal muscle

FEBS Letters ◽  
1976 ◽  
Vol 69 (1-2) ◽  
pp. 246-248 ◽  
Author(s):  
N.K. Nagradova ◽  
R.A. Asryants ◽  
N.V. Benkevich ◽  
M.I. Safronova
Keyword(s):  
Skeletal Muscle ◽  
Rat Skeletal Muscle ◽  
Arginine Residues

Skeletal muscle enzyme alterations after sprint and endurance training

1976 ◽  
Vol 40 (6) ◽  
pp. 868-871 ◽  
Author(s):  
R. C. Hickson ◽  
W. W. Heusner ◽  
W. D. Van Huss
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Vastus Lateralis ◽  
Rat Skeletal Muscle ◽  
Endurance Running ◽  
Muscle Enzyme ◽  
Lactate Dehydrogenase Activity ◽  
Different Types ◽  
Fumarase Activity ◽  
Over Time

Specifically designed programs of sprint and endurance running were used to determine how different types of training affect enzyme activities in selected energy metabolism pathways. Three types of rat skeletal muscle were studied. After 8 wk of training, small but significant decreases in lactate dehydrogenase activity (15%) were found in the soleus and white vastus lateralis muscles of the sprint animals. Decreased levels of phosphoglucomutase and lactate dehydrogenase (approx. 20%) of the white vastus lateralis muscles of the endurance group were observed at the same time. By 16 wk of training, fumarase activity increased approximately twofold in the white vastus muscles and 45% in the soleus and plantaris muscles of the endurance group. Similarly, increased fumarase activity (42%) was seen in the soleus muscles of the sprint group. In all muscles, phosphoglucomutase and lactate dehydrogenase activities generally were lower in the endurance animals than in the control animals. No significant differences were found between the sprint and endurance groups at either or sixteen weeks of training. These results suggest that similar enzyme adaptations occur over time with both types of training.

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