Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: HUMANGGP:009336 (ATPase)
 59,826 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myosin from rabbit stomach was highly purified by ammonium sulfate fractionation in the presence of ATP and MgCl2, ultracentrifugation and Sepharose 4B chromatography. The myosin composed of one heavy and two light chains as determined by SDS-gel electrophoresis. The molecular weights of the light chains were the same as those of gizzard myosin, about 20,000 and 17,000, respectively. The pH-activity curve and the KCl concentration dependency of Ca-ATPase of the stomach myosin were similar to those of other smooth muscle myosins. The stomach myosin was more resistant to pepsin digestion than skeletal myosin. Other proteolytic enzymes, trypsin, chymotrypsin, papain, and nagarse, digested the myosin in the same way as skeletal myosin.
 ...
PMID:Purification and some properties of rabbit stomach myosin. 1 37

The reactions of adenosine 14C-and gamma 32P-labelled ATP with isolated membranes from catecholamine storage vesicles of the bovine adrenal medulla were studied. In presence of Mg2+ about twice as much of 32P-radioactivity combined with the membrane as 14C-adenosine compounds at 31 degrees C and also at 0 degrees C, while in the absence of Mg2+ the amounts of 14C and 32P incorporated were similar for both substances. Autoradiography of the SDS-polyacrylamide gel after electrophoresis of the 32P-ATP-treated membrane protein showed two distinct zones corresponding to protein bands. Sonication released twice as much 32P-ATP as 14C-ATP from the space within the membrane particles indicating that at least half of the ATP present in space did not contain its original terminal phosphate group. About 40--45% of the 32P-radioactivity was incorporated in the membrane lipids, whereas only small amounts of 14C-radioactivity were extracted with lipids. About 1/3 of the incorporated 14C-radioactivity was not extractable with acids. The same amount remained in the 32P-ATP treated preparation acid-stably bound after extraction of the lipids and hus must be firmly bound ATP. When the reaction of the membrane preparation with labelled ATP was performed at 0 degrees C the fractions of the acid-stably bound 32P- and 14C-radioactivity increased. About 1 nmole/mg of protein (10--15%) of the bound 32P-radioactivity was exchangeable against unlabelled ATP, while only a very small fraction (less than 0.5 nmol/mg protein) of the 14C-radioactivity was exchanged against unlabelled ATP. Preincubation of the membrane particles with ATP-Mg2+ at 0 degrees C induced 30% inhibition of the ATPase activity and abolition of the net uptake of catecholamines. Different Km values obtained from initial velocity studies of ATPase activity and the overall-incorporation of 32P-radioactivity indicated that a direct correlation between these processes did not exist. Different strong inhibitory effects exerted by ADP on the ATPase activity and net uptake of catecholamine at the one hand and the overall 32P-and 14C-incorporation at the other hand supported that view. It is concluded that small fractions of the observed 32P-and 14C-incorporation can be involved in the ATP hydrolyzing reaction.
 ...
PMID:Distribution and metabolic fate of adenosine nucleotides in the membrane of storage vesicles from bovine adrenal medulla. 4 49

Plasma membranes were prepared from cultured Chinese hamster ovary cells utilizing a two-phase polymer system and were characterized by enzymatic and chemical assay, and by electron microscopy. The usual degree of purification of presumptive membrane markers such as Na+-K+ ATPase (ATP phosphohydrolase, EC 3.6.1.3) ranged from three-to eightfold. Gel electrophoresis in SDS revealed several polypeptides and two glycopeptides which were enriched in the plasma membrane fraction.
 ...
PMID:The isolation and characterization of the plasma membrane of cultured chinese hamster ovary cells. 12 93

Highly purified preparations of Streptococcus faecalis ATPase contain a similar but inactive protein detected by prolonged polyacrylamide gel electrophoresis. The inactive protein appears to arise by proteolytic cleavage of the major subunits in the enzyme. By use of a new technique, subunit analysis in SDS gels was performed on the enzyme band and the inactive protein band excised from a polyacrylamide gel after electrophoresis. The results indicated that the ATPase has the composition alpha3beta3gamma in which alpha = 60,000, beta = 55,000, and gamma = 37,000 daltons. The inactive protein appears to have the composition (f)6 in which f = 49,000 daltons. There is also evidence that the enzyme band contains some slightly modified forms of the ATPase, such as alpha3beta2 (f)gamma. The inactive protein lacks the capacity for tight nucleotide binding. Our experiments show that the tight ATPase-nucleotide complex formed in S. faecalis cells (the endogenous complex) behaves differently from the tight complex formed in vitro (the exogenous complex). We prepared a doubly labeled complex containing endogenous 32P-labeled ADP and ATP and exogenous 3H-labeled ADP. We observed that the addition of free nucelotide to the doubly labeled ATPase displaced the exogenous bound ligand from the enzyme but not the endogenous bound nucleotide. We suggest that the displaceable and nondisplaceable forms of the tight ATPase-nucleotide complex correspond to two different conformational states of the enzyme.
 ...
PMID:Studies of substructure and tightly bound nucleotide in bacterial membrane ATPase. 12 88

Solution of thrombosthenin, the contractile protein complex isolated from pig platelets, have been studied by analytical ultracentrifugation and zone sedimentation in sucrose density gradients. Freshly prepared thrombosthenin in 0.6 M KCl shows a prominent peak in the ultracentrifuge with S degrees 20w about 5.5 and higher molecular weight aggregates (greater than 100S) sedimenting quickly to the bottom of the cell. Short term storage of high ionic strength solutions of thrombosthenin induces actomyosin-like gel formation and these gels dissociate with ATP and Mg2+ ions into two components of S degrees 20w 8.0 and S degrees 20w50. The supernatant, after actomyosin gel removal, contains only the S degrees 20w5.5 protein. From results of Ca2+ ATPase activity measurements and SDS polyacrylamide gel electrophoretic mobilities of dissociated thrombosthenin separated into fractions in sucrose density gradients, it is concluded that the S degrees20w5.5 protein species is the myosin-like protein of thrombosthenin. The S degrees 20w8.0 protein is not fibrinogen but also has myosin-like properties and is believed to be myosin dimer. Species of higher S values seen in the presence of ATP and Mg2+ in the analytical ultracentrifuge and located in the higher density zones of the sucrose gradients all gave in SDS polyacrylamide gel electrophoresis a single band of molecular weight 46-47,000 daltons. These subunit proteins appear to be derived from a range of polymeric variants of the F-actin-like protein of the contractile complex. All these higher density F-actin-like proteins readily form superprecipitates and display syneresis when combined with rabbit skeletal muscle myosin or platelet myosin. They are also all capable of conferring upon these two myosins a Mg2+ activated ATPase activity. It is suggested that in thrombosthenin solutions a myosin monomer-dimer equilibrium state exists which can be directionally influenced by a number of factors. The coexistence in the solution of F-actin and Mg2+ ATP, for example, increases the propensity of the myosin-like protein to form the higher molecular weight aggregate. Such aggregation may be the initiating mechanism for the intracellular organization of the thick filaments of the actomyosin complex, preparatory to a contractile event.
 ...
PMID:Platelet contractile proteins: separation and characterization of the actin and myosin-like components. 12 96

The subunit composition, the thiol group content and the biological activities of cardiac tropomyosins (TM) of various animal species were compared. Cardiac TM from small animals such as rabbit, guinea-pig, rat and dog contain 2 SH/mole and were resolved into one band on SDS and acid urea electrophoresis and into two bands on alkaline urea electrophoresis. Chicken cardiac TM likewise gave one band and it contains 4 SH/mole. In contrast pig, sheep and human cardiac TM contain respectively 2.6, 2.4, and 2.4 SH/mole and were resolved into two bands alpha and beta on the different electrophoresis systems used, with a beta:alpha ratio respectively of I:4.2, I:4.6, I:4.8. The alpha-TM components from sheep skeletal and pig and sheep cardiac muscles were more positively charged than the rabbit skeletal alpha-TM component, as shown in alkaline urea electrophoresis system. The alphaalpha and alphabeta combinations of dimers found for skeletal muscle by other authors, were also found for cardiac pig TM. All the TM have the same effect on the Ca2+-stimulated ATPase activity of desensitized actomyosin (DAM) and on the Mg2+-stimulated ATPase activity of DAM with troponin-complex. This work suggests that the subunits of the TM from skeletal and cardiac muscles are heterogenous in their M.W. and their charges and that in the heart as well as in skeletal muscle a relationship seems to exist between the amount of the beta component and the speed of contraction of the muscle: a higher amount of this component was found in the bulky hearts which are also those which contract slower.
 ...
PMID:A comparative study of skeletal and cardiac tropomyosins: subunits, thiol group content and biological activities. 13 Dec 98

The relaxing protein (TM-TN complex) was isolated from plasmodia of Physarum. SDS-gel electrophoresis revealed that the relaxing protein consists of tropomyosin subunits with a molecular weight of 35,000 troponin subunits with molecular weights of 38,000 (T) and 24,000 (I) and several other components. No component corresponding to muscle troponinC (MW-18,000) was detected in the plasmodium relaxing protein. The relaxing protein combined with muscle F-actin, and inhibited the ATPase [EC 3.6.1.3] activity and superprecipitation of reconstituted muscle actomysin in the absence of Ca2+ ions. The inhibition was reversed by adding 1 muM Ca2+ ions.
 ...
PMID:Physarum tropomyosin-troponin complex. Isolation and properties. 13 91

The ATPase activity of actomyosin prepared from taenia coli muscle of guinea pig was found to increase upon adding rabbit skeletal heavy meromyosin (HMM) in the absence of Ca2+. SDS-gel electrophoresis of muscle homogenates did not reveal the presence of troponin. Ca2+-regulation in taenia coli muscle thus appears to be myosin-linked. The glycerinated muscles which did not develop any tension in the presence of EGTA contracted after irrigation with rabbit skeletal myosin. Skeletal HMM could also cause tension generation in strips of glycerinated taenia coli in the presence of EGTA. The tension developed by the muscles in the presence of Ca2+ was increased if HMM was added. The HMM-induced tension was associated with a marked increase in ATPase activity both in the presence and in the absence of Ca2+. No HMM-associated tension could be detected when inactivated HMM was employed or when MgATP was substituted with Mg-pyrophosphate or Mg-AMP-PNP. The mechanical effect of HMM probably results from a mechanochemical interaction between the added HMM and muscle actin.
 ...
PMID:Evidence for myosin-linked regulation in guinea pig taenia coli muscle. 13 41

The present studies concern the roles of synthesis and degradation of the large subunit of (Na+ + k+)-adenosine triphosphatase (NaK-ATPase) in the response to triiodothyronin (T3). Single doses of either the diluent of T3 (50 mug/100 g body weight) were given to two pairs of surgically thyroidectomized rats. Twenty hours after injection, the rats received 3H- or 35S-labeled methionine administered as a constant injusion into the tail vein for 1 h. The kidneys were removed either 8 h or 20 h after infusion and the eight kidneys were divided into pairs, as follows. I, 3H (diluent)/35S (T3); II, 35S (diluent)/3H (T3); III, 3H (diluent)/35S (diluent); IV, 3H (T3)/35S (T3). Partially purified NaK-ATPase was prepared from the pooled homogenates and prepared from the pooled homogenates and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAG-electrophoresis). The large subunit of NaK-ATPase was identified by (Na+ + mg2+)-dependent and K+-sensitive incorpotation of 32P from [gamma-32P]ATP. This component had an estimated molecular weight of 92,000 and migrated as a single peptide in gels of varying total carylamide concentration, with respect to: (1) Coomassie blue staining, (b) (Na+ + Mg2+)-dependent, K+-sensitive incorporation of 32P from [gamma-32-P]ATP, and (c) T3-dependent enhanced incorporation of labeled methionine. T3 augmented incorporation of labeled methionine into the large subunit by 44% 8 h after infusion of the amino acid and by 61% 20 h after infusion. Incorporation of methionine into two adjacent polypeptides in the SDS gels was unaffected by thyroid status. The effect otical NaK-ATPase was assessed by a double label technique. Pairs of thyroidectomized rats were injected with either the diluent or 50 mug of T3/100 g body weight at 48-h after the first injection (diluent or T3, i.e. Day "zero"). Kidney cortices were processed on either Day 4 or Day 6; the partially purified NaK-ATPase fraction was prepared, labeled with [gamma-32P]ATP, and analyzed by SDS-PAG-electrophoresis. The degredation rate constants of the large subunit were similar; 0.145 and 0.124 day-1 for the hypothyroid and T3-treated groups, respectively. Thus, the T2-dependent increase in incorporation of labeled methionine into the large subunit appears to result from enhanced synthesis and this increase is sufficient to account for the entire increase in both the number of the activity of the NaK-ATPase units.
 ...
PMID:Effect of triiodothyronine on the synthesis and degradation of renal cortical (Na+ + k+)-adenosine triphosphatase. 13 43

During Mn(II)-ATP hydrolysis by myosin, the predominant intermediate formed at the burst site of the enzyme below 10 degrees is the myosin-ADP complex formed by adding ADP to myosin, while above 10 degrees it is the myosin -ADP-P1 complex generated by ATP hydroolysis (Yazawa, Morita, & Yagi (1973) J. Biochem. 74, 1107; Hozumi & Tawada (1975) Biochim. Biophys. Acta 376, 1; Tawada & Yoshida (1975) J. Biochem. 78, 293). It is suggested that the second (non-burst) site of myosin predominantly forms the myosin-ATP complex (Hozumi & Tawada, ibid.). From these findings, it is expected that (i) myosin subfragment 1 (S1) having the burst site is bound to actin in Mn(II)-ATP solution containing ADP below 10 degrees, because it forms the S1-ADP complex even in the presence of ATP; (ii) the other S1, i.e., that having the non-burst site, is dissociated from actin, because it forms the S1-ATP complex. These two expectations were confirmed by viscosity measurements of acto-S1 solutions, giving a basis for the separation of S1 into two fractions: one having the burst site and the other having the non-burst site. S1 having the non-burst site could be extracted from partially papain [EC 3.4.22.2]-digested myofibrils of rabbit skeletal muscle with a solution containing MnCl2, ATP, and ADP at 0 degrees. S1 having the burst site was extracted from myofibrils already used for the extraction of S1 having the non-burst site, with a solution containing MgCl2 and ATP at 20 degrees. The former S1 fraction had Mg-ATPase [EC 3.6.1.3] activity, but scarcely showed any initial burst of Pi liberation. The latter S1 showed a Pi burst of more than 0.5 (M/M). The steady state ATPase activity of the former S1 was slightly higher than that of the latter. The burst size of normal S1, i.e., that extracted from papain-digested myofibrils with Mg-PPi or Mg-ATP, was 0.5 (M/M). The ultraviolet absorption spectrum of the non-burst type S1 was not changed by ADP but was changed by ATP, though the difference spectrum was distinct from that of normal S1 and the difference molar extinction coefficient at 289 nm was only 20% of that of normal S1. No significant difference was seen in the compositions of these two S1's and normal S1, as determined by SDS gel electrophoresis.
 ...
PMID:Separation of myosin subfragment 1 into two fractions, one having the burst site and the other having the non-burst site. 13 98


1 2 3 4 5 6 7 8 9 10 Next >>