Direct Relationship of Phosphorylase and Mitochondrial α-Glycerophosphate Dehydrogenase Activity in Skeletal Muscle

Nature ◽  
1961 ◽  
Vol 191 (4787) ◽  
pp. 504-504 ◽  
Author(s):  
A. G. E. PEARSE
Author(s):  
З.С. САНОВА

В статье представлены материалы о взаимосвязи продолжительности продуктивного использования коров с характеристикой устойчивости к деградации, с возрастом отела и удоем. В исследованной, разнородной по происхождению, группе животных для прогноза продуктивного периода коров, обусловленного устойчивостью к деградации и возрастом первого отела, пригодно уравнение регрессии, аргументами в котором являются индекс устойчивости, возраст первого отела в первой и второй степенях. Коэффициент корреляции межу предсказанными значениями продуктивного периода и его фактическими величинами в I группе составляет 0,502, во II - 0,604. При этом крайние варианты прогнозируются со статистическими ошибками 5 мес при оценке индекса устойчивости по 2 лактациям и 4,1 мес по 3, а средние варианты, соответственно, 1,6 и 1,51 мес. Индекс устойчивости к процессу старения является важной характеристикой биологических особенностей коров, определяющий их продуктивное долголетие. Его оценка по первым 2 и 3 лактациям имеет прямолинейную связь с продуктивным периодом (r=0,4109 и r=0,5270), соответственно. Зависимость продуктивного периода от возраста первого отела криволинейная — с увеличением возраста первого отела сокращается срок продуктивного использования, при возрасте первого отела более 1400 дней срок продуктивного использования колеблется от 1,33 до 1,41 лактации. Коэффициент корреляции между этими характеристиками коров составляет - 0,2164 в I и - 0,2620 во II группах. The article presents materials about the relationship of the duration of productive use of cows with the characteristic of resistance to degradation, with the age of calving and milk yield. In the studied group of animals, which is heterogeneous in origin, the regression equation is suitable for predicting the productive period of cows due to resistance to degradation and the age of the first calving, the arguments of which are the stability index, the age of the first calving in the first and second degrees. The correlation coefficient between the predicted values of the productive period and its actual values in group I is 0.502, in group II - 0.604. At the same time, the extreme variants are predicted with statistical errors of 5 months when evaluating the stability index for 2 lactations and 4.1 months for 3, and the average variants, respectively, are 1.6 and 1.51 months. The index of resistance to the aging process is an important characteristic of the biological characteristics of cows, which determines their productive longevity. Its estimate for the first 2 and 3 lactations has a direct relationship with the productive period (r=0.4109 and r=0.5270), respectively. The dependence of the productive period age at first calving curvilinear with increasing age at first calving reduces the time to productive use, while age at first calving of more than 1400 days, the period of productive use ranges from 1.33 to 1.41 lactation. The correlation coefficient between these characteristics of cows is-0.2164 in I and-0.2620 in II groups.


1976 ◽  
Vol 158 (2) ◽  
pp. 203-210 ◽  
Author(s):  
S A Hagg ◽  
S I Taylor ◽  
N B Ruberman

1. The interconversion of pyruvate dehydrogenase between its inactive phosphorylated and active dephosphorylated forms was studied in skeletal muscle. 2. Exercise, induced by electrical stimulation of the sciatic nerve (5/s), increased the measured activity of (active) pyruvate dehydrogenase threefold in intact anaesthetized rated within 2 min. No further increase was seen after 15 min of stimulation. 3. In the perfused rat hindquarter, (active) pyruvate dehydrogenase activity was decreased by 50% in muscle of starved and diabetic rats. Exercise produced a twofold increase in its activity in all groups; however, the relative differences between fed, starved and diabetic groups persisted. 4. Perfusion of muslce with acetoacetate (2 mM) decreased (active) pyruvate dehydrogenase activity by 50% at rest but not during exercise. 5. Whole-tissue concentrations of pyruvate and citrate, inhibitors of (active) pyruvate dehydrogenase kinase and (inactive) pyruvate dehydrogenase phosphate phosphatase respectively, were not altered by excerise. A decrease in the ATP/ADP ratio was observed, but did not appear to be sufficient to account for the increase in (active) pyruvate dehydrogenase activity. 6. The results suggest that interconversion of the phosphorylated and dephosphorylated forms of pyruvate dehydrogenase plays a major role in the regulation of pyruvate oxidation by eomparison of enzyme activity with measurements of lactate oxidation in the perfused hindquarter [see the preceding paper, Berger et al. (1976)] suggest that pyruvate oxidation is also modulated by the concentrations of substrates, cofactors and inhibitors of (active) pyruvate dehydrogenase activity.


1991 ◽  
Vol 278 (2) ◽  
pp. 375-380 ◽  
Author(s):  
T L Kirley

The Mg(2+)-ATPase present in rabbit skeletal-muscle transverse tubules is an integral membrane enzyme which has been solubilized and purified previously in this laboratory [Kirley (1988) J. Biol. Chem. 263, 12682-12689]. The present study indicates that, in addition to the approx. 100 kDa protein (distinct from the sarcoplasmic-reticulum Ca(2+)-ATPase) seen previously to co-purify with the Mg(2+)-ATPase activity, there are also proteins having molecular masses of 160, 70 and 43 kDa. The 70 and 43 kDa glycosylated proteins (50 and 31 kDa after deglycosylation) are difficult to detect by SDS/PAGE before deglycosylation, owing to the broadness of the bands. Additional purification procedures, cross-linking studies and chemical and enzymic deglycosylation studies were undertaken to determine the structure and relationship of these proteins. Both the 97 and 160 kDa proteins were demonstrated to be N-glycosylated at multiple sites, the 97 kDa protein being reduced to a peptide core of 84 kDa and the 160 kDa protein to a peptide core of 131 kDa after deglycosylation. Although the Mg(2+)-ATPase activity is resistant to a number of chemical modification reagents, cross-linking inactivates the enzyme at low concentrations. This inactivation is accompanied by cross-linking of two 97 kDa molecules to one another, suggesting that the 97 kDa protein is involved in ATP hydrolysis. The existence of several proteins along with the inhibition of ATPase activity by cross-linking is consistent with the interpretation of the susceptibility of this enzyme to inactivation by most detergents as being due to the disruption of a protein complex of associated subunits by the inactivating detergents. The 160 kDa glycoprotein can be partially resolved from the Mg(2+)-ATPase activity, and is identified by its N-terminal amino acid sequence as angiotensin-converting enzyme.


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