Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Forty-five Large White barrows were injected daily i.m. with either excipient from 30 to 100 kg BW (CTRL), excipient from 30 to 60 and porcine somatotropin (pST; 100 micrograms/kg BW) from 60 to 100 kg BW (pST-60), or pST (100 micrograms/kg BW) from 30 to 100 kg BW (pST-30). Somatotropin accelerated overall growth rate (+4 and +9% for pST-60 and pST-30, respectively), increased longissimus (+10.3 and +14.7%) and semitendinosus (+17 and +13%) muscle weights, and decreased backfat (-49 and -58%) and leaf fat (-49 and -53%) weights. The administration of pST resulted in a similar increase in muscle fiber size for all fiber types in both longissimus (LM) and semispinalis (SS) muscles (+21%). Somatotropin had otherwise little effect on muscle fiber types and biochemical traits of LM, whereas dramatic changes were observed in SS. The relative area occupied by Type IIB fibers was increased (+22 and +29%) and that of Type I fibers was decreased (-10 and -15%). In pST-30 animals, myosin ATPase activity (+15%) and native myosin fast isoform proportion (+10%) were augmented, and energy metabolism was more glycolytic (lactate dehydrogenase: +25%) and less oxidative (citrate synthase: -13%; beta-hydroxyacyl-CoA dehydrogenase: -21%). Compared to CTRL animals, administration of pST increased muscle water concentration (LM: +.8 and +1.1%: SS: +3.3 and +3.3%) and decreased intramuscular fat (LM: -29 and -27%; SS: -39 and -50%). The pH measured 45 min and 24 h postmortem, glycogen content, reflectance, and index of light diffusion were mostly not affected by pST treatment. In conclusion, pST had a very favorable effect on growth performance without any important effect on meat quality traits except for the reduction in intramuscular lipid content. The results indicated that the effects of pST on muscular histochemical and biochemical characteristics were different in LM and SS muscles.
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PMID:Performance, plasma hormones, histochemical and biochemical muscle traits, and meat quality of pigs administered exogenous somatotropin between 30 or 60 kilograms and 100 kilograms body weight. 145

1. Cross sections from the middle of the gluteus medius were removed from 10 adult horses and used to evaluate changes in histochemically determined muscle fiber type and biochemically determined metabolic enzyme activities as a function of sample depth. 2. Muscle fiber types determined using histochemical methods for myosin ATPase (pH 9.4) and succinic dehydrogenase (SDH) activity indicated percent fast-twitch glycolytic (FG) muscle fibers decreased and slow-twitch oxidative (SO) fibers increased as a function of increasing sampling depth. 3. Percent histochemically determined fast-twitch oxidative glycolytic (FOG) fibers decreased slightly only in the deepest region of the gluteus medius. 4. Citrate synthase (CS) enzymatic activity, used as a marker for mitochondrial oxidative potential, increased 2.5-fold in activity per g of muscle protein from 1 to 8 cm sampling depth. 5. 3-hydroxyacyl-CoA dehydrogenase (HAD) enzymatic activity, used as a marker for lipid oxidation potential, increased 3-fold in activity per g of muscle protein when the depth increased from 1 to 8 cm. 6. Phosphorylase (PS) enzymatic activity, used as a marker for potential glycogen utilization, decreased 50% in activity per g of muscle protein when going from 1 to 8 cm. 7. Lactate dehydrogenase (LDH) enzymatic activity, used as a marker for anaerobic glycolytic potential, decreased about 50% in activity as the sampling depth increased from 1 to 8 cm. 8. In summary, the superficial portion of the equine gluteus medius was found to be more glycolytic and less aerobic in its metabolic profile than deeper regions. The muscle became progressively more aerobic and less glycolytic with increasing sampling depth.
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PMID:Changes in the metabolic profile of the equine gluteus medius as a function of sampling depth. 290 49