In the presence of NH 4 Cl and hypotonic solutions, Rana balcanica red cells respond by increasing their volume. The stimulation of cellular volume by hypotonicity is more rapid than that of NH 4 Cl, while the maximum value is less than that observed in the presence of NH 4 Cl. Depending on the caus
Glycolytic enzyme activity in developing red and white muscle
β Scribed by R. H. Dalrymple; R. G. Cassens; L. L. Kastenschmidt
- Publisher
- John Wiley and Sons
- Year
- 1974
- Tongue
- English
- Weight
- 558 KB
- Volume
- 83
- Category
- Article
- ISSN
- 0021-9541
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The activities of the constant proportion enzymes of the EmbdenβMeyerhof chain (triose phosphate isomerase (TIM), glyceraldehydeβ3βphosphate dehydrogenase (GAPDH), phosphoglycerate kinase (PGK), phosphoglycerate mutase (PGM) and enolase (ENOL)), and the activity of lactic dehydrogenase (LDH) were studied in developing red (trapezius) and white (longissimus) muscles of the pig from a fetal stage to 24 weeks postnatal. Both muscles were differentiated by two weeks postnatal in the sense that they had reached the adult level of enzyme activity. Enzyme activities were twoβ to threeβfold greater in the longissimus than in the trapezius. Enzyme activity ratios based on GAPDH were not consistent in the fetal and day 1 samples but were consistent during later stages of growth. Ratios of enzyme activity based on activity at 105 days gestation revealed that TIM, PGK and PGM are grouped and follow the same pattern, but GAPDH and ENOL are quite different from each other and from the pattern shown by TIM, PGK and PGM. The constant proportion concept in developing muscle is therefore questioned.
π SIMILAR VOLUMES
## Abstract In the fastβgrowing Atlantic cod (__Gadus morhua__), the specific activities of the glycolytic enzymes phosphofructokinase (PFK), pyruvate kinase (PK), and lactate dehydrogenase (LDH) in white muscle were positively correlated with growth rate. For PFK and PK, season modified the relati
An investigation of the effects of ethanol on both the stabilities and activities of glycolytic enzymes of yeast and Zymomonas mobilis is presented. It is concluded that enzyme denaturation is unlikely to play a direct part in ethanol tolerance, but inhibition by ethanol may be responsible for slow