Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A protein has been studied which spontaneously precipitates from stored fractions of platelet soluble phase prepared by density gradient centrifugation. It is rich in a Ca2+ ATPase activity which displays an activity/pH profile resembling that of skeletal muscle myosin. Adjustment of freshly prepared soluble phase fractions to 0.6 M with respect to KCl and dilution 1 in 3 results in the precipitations of a protein fraction with essentially the same enzymatic properties as the spontaneously precipitable protein. These two similar proteins represent between 9 and 13% of the soluble phase total protein and each account for almost the whole of divalent cation activated ATPase activity of the soluble phases from which they were derived. The Mg2+ ATPase activity is only about twice purified with respect to the soluble phase enzyme activity, but the Ca2+ ATPase shows a 10-13-fold enrichment. Synthetic actomyosins can be prepared from the two proteins by addition of either platelet or skeletal muscle actin. These show significant increases in Mg2+ ATPase at the most favourable combination ratios. The ratio between the yield of soluble phase protein obtained by dilution precipitation and the lactate dehydrogenase activity of the soluble phase remains constant under a wide range of homogenization and sonication conditions applied to the original whole platelet suspensions. This confirms our earlier view that the soluble phase is a valid intracellular compartment for a considerable proportion of the platelet contractile protein and that in the complex the myosin-like component predominates.
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PMID:The identification and subcellular localization of thrombosthenin "M", the myosin-like component of pig platelets. 0 43

The adenosine triphosphatase (ATPase) activities of human polymorphonuclear leukocytes (PMNL) were studied with an assay that monitored the release of 32P-labeled inorganic pyrophosphate (32P1) from gamma-[32P]adenosine 5'-triphosphate (ATP). In cell homogenates, (Na+ + K+)-sensitive, ouabain-inhibitable ATPase comprised an insignificant fraction of the total ATPase activity. Additions of p-nitrophenyl phosphate and beta-glycerophosphate (substrates for nonspecific acid and alkaline phosphatases) and of tartrate (inhibitor of acid phosphatase) gave no indication of inhibition. This suggested that the assay was relatively specific for ATP hydrolysis. The activity was found to have a pH optimum of 8.7 and a Km for ATP of 0.6 mM. There was an absolute requirement for Mg2+, with other divalent cations substituting less efficiently. When the Mg2+-dependent ATPase activity of intact cells was compared with that in homogenized cells, no significant difference was observed. The activity in intact cells was linear with respect to incubation time up to at least l0 min. Trypan blue staining and lactate dehydrogenase assays revealed that greater than 92% of the PMNL remained intact and viable during the assay. No soluble ATPase was released from the cells under assay conditions. In following the distribution of gamma[32P]ATP and 32P2 counts became cell associated. Since the experimental evidence supports the observation that PMNL remain intact and viable and that ATP does not penetrate the cell under assay conditions, it is proposed that greater than 90% of the Mg2+-dependent ATPase of the human PMNL is associated with a plasma membrnae enzyme. This would qualify the enzyme for the role of a plasma membrane marker for future fractionation and isolation attempts.
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PMID:Magnesium-dependent adenosine triphosphatase as a marker enzyme for the plasma membrane of human polymorphonuclear leukocytes. 1 92

Histochemical techniques have been employed to characterize enzymatic activity in the mesocoxal muscles of the cockroach, Periplaneta americana. Through our studies of the enzymes myosin-ATPase, NADH reductase, succinic dehydrogenase (SDH), and lactic dehydrogenase (LDH), we were able to classify fibers within these muscles according to criteria established for muscle fibers of vertebrates. Many of the mesocoxal muscles possess two different and distinct populations of fibers, whereas the remaining muscles are homogeneous with respect to their constituent fibers. The data presented here indicate biochemical heterogeneity for muscles of differing structural and functional features and possible neurotrophic influences upon oxidative enzymes and myosin-ATPase isozymes.
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PMID:Enzyme histochemistry of the mesocoxal muscles of Periplaneta americana. 3 9

The case of a 35 years-old man, with chronic proximal muscle atrophy in which at the muscle biopsy tubular aggregates were found by histochemistry procedures is reported. The tubular aggregates stained positive with the modified Gomori trichrome, haematoxylin-eosin, DPNH-diaphorase, non specific esterases, phosphorylase, P.A.S., oil red O and lactate dehydrogenase. They did not show in the routine and acid pre-incubated ATPase, acid and alkaline phosphatases and succinate dehydrogenase. Only found in type II fibers. A brief discussion about the pathogenesis and function of the tubular aggregates is made. The authors believe that the tubular aggregates in this case are secondary to prolonged use of phenobarbital and diphenylhydantoin, associated with the basic denervation process and alcohol abuse.
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PMID:[Tubular aggregates in a case of chronic proximal spinal atrophy]. 8 34

1. The effects of ouabain on renin secretion by rat renal cortical slices were studied. 2. Renin secretion was inhibited by 10(-3) M-ouabain in the presence of free Ca (10(-4) to 2.6 x 10(-3) M). Inhibition was blocked at Ca less than 10(-8) M. 3. The effect of free Ca on ouabain-inhibition was shown to be independent of the presence of EGTA, completely reversible, and unrelated to passive leakage of renin from non-viable cells, as assessed by simultaneous release of lactate dehydrogenase activity (LDH). 4. It is proposed that, as a result of inhibition of Na, K-ATPase by ouabain, (a) intracellular Na increases in the renin-secreting juxtaglomerular cells, (b) intracellular Ca increases, via an Na-Ca exchange mechanism, and (c) that Ca accumulation, in some unknown manner, inhibits renin secretion.
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PMID:Possible mechanism of the inhibitory effect of ouabain on renin secretion from rat renal cortical slices. 11 99

The biochemical effects of the nonsteroidal compound Centchroman were observed in healthy, adult, female rhesus monkeys. The compound was administered at the antifertility dose (.625 mg/kg) for 22 days in a cycle. No marked weight changes were seen in the Fallopian tube, ovary, adrenal or pituitary as a result of treatment. Uterine weight increased significantly, however (p less than .01). In the Fallopian tube, levels of glycogen and protein increased significantly (p less than .01), lactic acid decreased significantly (p less than .01), and nonprotein nitrogen was unchanged as a result of treatment. Similar changes were observed in the uterus, and in addition, total total phospholipid concentration rose significantly (p less than .01) in the uterus. The activities of beta-glucuronidase, acid and alkaline phosphatases and glucose-6-phosphate dehydrogenase (G-6-PD) in the Fallopian tube were unchanged due to treatment. Adenosine triphosphatase (ATPase) and malic dehydrogenase activities were significantly stimulated (p less than .01) and lactic dehydrogenase activity was significantly depressed (p less than .01). In the uterus, beta-glucuronidase and acid and alkaline phosphatase activity were unaltered, however, the activities of ATPase and the dehydrogenases of glucose-6-phosphate, lactate and malate were markedly increased (p less than .01). It is suggested that the antifertility effect of Centchroman may be due principally to the ability of the compound to elicit estrogen-like responses in the Fallopian tube and uterus.
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PMID:Effect of 3,4-trans-2,2-dimethyl-3-phenyl-4-P-(beta-pyrrolidinoethoxy) phenyl -7-methoxy chroman (centchroman) on the biochemistry of the fallopian tube and uterus of rhesus monkeys (Macaca mulatta). 12 88

The effects of the nonsteroidal title compound (DBF) on the biochemical composition of the Fallopian tube and uterus were studied in the rhesus monkey. Monkeys received 2 mg/kg daily by mouth, which is the antifertility dose. The weight of the pituitary was significantly decreased (p less than .05) due to treatment, but the weights of the Fallopian tube, uterus, ovary and adrenal were unaltered. In both the Fallopian tube and uterus, DBF induced a significant increase (p less than .01) in the concentration of glycogen, protein and nonprotein nitrogen, and a significant decrease (p less than .01) in the concentration of lactic acid. The total phospholipid level in the uterus showed an increase (p less than .01) in the activities of adenasine triphosphatase (ATPase), malic dehydrogenase, acid and alkaline phosphatases, and glucose-6-phosphate dehydrogenase (G-6-PD) was seen. Lactic dehydrogenase activity fell (p less than .01) and the activity of beta-glucuronidase was unchanged. In the uterus, ATPase, malic dehydrogenase, alkaline phosphatase and lactic dehydrogenase activities increased significantly (p less than .01), beta-glucuronidase and acid phosphatase activities fell (p less than .01) and G-6-PD activity was unaltered. The antifertility effect of DBF may be due to its ability to elicit many biochemical effects similar to those induced by a typical estrogen.
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PMID:Effect of 2-phenyl-3-p-(beta-pyrrolidinoethoxy) phenyl-beta-methoxy benzofuran hydrochloride (DBF) on the biochemistry of the fallopian tube and uterus of rhesus monkey (Macaca mulatta). 12 89

In the gastrocnemius muscle of cat and rat, staining for oxidative enzymes differentiated three fiber types (A,B,C) and staining for adenosine triphosphate at pH 9.4 differentiated two fiber types (I, II) with a reliability of 90% and 98%, respectively. In cat 96% and in rat 90% of the fibers were typed identically after staining for nicotinamide adenine dinucleotidelinked lactic dehydrogenase (LDH) and succinic dehydrogenase (SDH). When differentiated by staining for LDH, A and B fibers were of type I. IN RAT, 80-90% OF ALL FIBERS WERE OF TYPE 22, COMPPRISING A, B and C fibers. Type I fibers stained for LDH intensely as did C fibers of type II, but stained intermediately for SDH. The degree of staining was measured by photometry. When fibers were stained for LDH, histograms of density showed three peaks corresponding to A, B and C fibers in cat, but only two peaks corresponding to A and C fibers in rat, In cat and rat, the densities of A, B and C fibers belonged to different populations. In soleus muscle of cat and rat stained for LDH, menadione-linked alpha-glycerophosphate dehydrogenase and adenosine triphosphatase at pH 9.4, the degree of staining differed from thatin any type of fiber in gastrocnemius muscle
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PMID:Histochemical fiber typing and staining intensity in cat and rat muscles. 12 97

The activities of the Na+--K+-ATPase, succinic dehydrogenase (SDH/, lactic dehydrogenase (LDH/ and glucose-6-phosphat dehydrogenase (G-6-PDH/ were studied in the cortex outer and inner medulla of the kidneys of rats with spontaneous hypertension (SHR) and were compared with those of control normotensive Wistar rats. The SHR aged 6--8 weeks had durint the prehypertensive and the early hypertensive stage the same enzymatic activities as control rats. Rats with a steady SH aged 16-22 weeks had low specific activity of the, Na+--K+-ATPase, SDH and LDH in the outer medulla. The latter can be associated with decreased intensity of the energy metabolism and a reduction of the active sodium transport in the ascending limb of the loop of Henle in the SHR rats and cold cause the phenomenon of exaggerated natriuresis characteristic of hypertension.
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PMID:[Na+--K+-adenosine triphosphatase and some oxidoreductases in the kidney of rats with spontaneous hypertension]. 12 6

Muscle samples were obtained from the gastrocnemius of 17 female and 23 male track athletes, 10 untrained women, and 11 untrained men. Portions of the specimen were analyzed for total phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) activities. Sections of the muscle were stained for myosin adenosine triphosphatase, NADH2 tetrazolium reductase, and alpha-glycerophosphate dehydrogenase. Maximal oxygen uptake (VO2max) was measured on a treadmill for 23 of the volunteers (6 female athletes, 11 male athletes, 10 untrained women, and 6 untrained men). These measurements confirm earlier reports which suggest that the athlete's preference for strength, speed, and/or endurance events is in part a matter of genetic endowment. Aside from differences in fiber composition and enzymes among middle-distance runners, the only distinction between the sexes was the larger fiber areas of the male athletes. SDH activity was found to correlate 0.79 with VO2max, while muscle LDH appeared to be a function of muscle fiber composition. While sprint- and endurance-trained athletes are characterized by distinct fiber compositions and enzyme activities, participants in strength events (e.g., shot-put) have relatively low muscle enzyme activities and a variety of fiber compositions.
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PMID:Skeletal muscle enzymes and fiber composition in male and female track athletes. 12 49


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