By the method of second quantization we construct an infinite-dimensional graded module for the centralizer of an involution of the fischer-Griess "Monster" simple group f(1) so that the Thompson series are ...
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By the method of second quantization we construct an infinite-dimensional graded module for the centralizer of an involution of the fischer-Griess "Monster" simple group f(1) so that the Thompson series are those conjectured by Conway and Norton. As a consequence we obtain some identities and congruences relating modular functions j and eta. We are hopeful that this representation can be extended to the whole group f(1), proving all the conjectures by Conway and Norton in their recent paper [Conway, J. H. & Norton, S. P. (1979) Bull. London Math. Soc. 11, 308-339].
f1-ATPase was extracted by the diphosphatidylglycerol procedure from bovine heart mitochondrial ATPase complexes that differ in ATPase activity, cold stability, ATPase inhibitor and Mg content. The ATPase activity of ...
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f1-ATPase was extracted by the diphosphatidylglycerol procedure from bovine heart mitochondrial ATPase complexes that differ in ATPase activity, cold stability, ATPase inhibitor and Mg content. The ATPase activity of the isolated enzymes was dependent upon the activity of the original particles. f1-ATPase extracted from submitochondrial particles prepared in ammonia (pH 9.2) and filtered through Sephadex G-50 was comparable to the enzyme purified by conventional procedures. f1-ATPase extracted from submitochondrial particles prepared in the presence of Mg and ATP at neutral pH was similar to factor A. No systematic relationship was found between the ATPase inhibitor content and ATPase activity of these f1-ATPase preparations. A relationship was observed between this activity and the efficiency of the ATPase inhibitor-f1-ATPase associaton within the membrane. The ATPase activity of isolated f1-ATPase reflects the properties of original ATPase complex provided a rapid and not denaturing procedure of isolation is employed.
A simple technique of purification of the soluble pig heart mitochondrial f1-ATPase is described. It consists of removal of extrinsic proteins from mitochondrial membranes before extraction with chloroform and ammoniu...
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A simple technique of purification of the soluble pig heart mitochondrial f1-ATPase is described. It consists of removal of extrinsic proteins from mitochondrial membranes before extraction with chloroform and ammonium sulfate fractionation. A high degree of purity, an excellent stability and a good yield are attained after gel filtration through an Ultrogel ACA 34 column equilibrated in the presence of 50% glycerol. The tested properties of the f1-ATPase prepared by this method are similar to those of the same enzyme extracted by sonication. The enzyme is virtually devoid of tightly bound nucleotides. Some characteristics of the behavior of the .beta. subunit are shown.
The latent coupling factor (f1)-ATPase of M. lysodeikticus [luteus] was purified to homogeneity as determined by a number of criteria including non-denaturing polyacrylamide gel electrophoresis, crossed immunoelectrop...
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The latent coupling factor (f1)-ATPase of M. lysodeikticus [luteus] was purified to homogeneity as determined by a number of criteria including non-denaturing polyacrylamide gel electrophoresis, crossed immunoelectrophoresis and analytical ultracentrifugation. By inclusion of 1 mM phenylmethyl sulfonyl fluoride, a serine protease inhibitor, in the shock-wash step of release off1 from the membranes, the spontaneous activation of both crude and purified ATPase by endogenous membrane protease(s) could be prevented, thereby yielding a highly latent ATPase preparation. Equilibrium ultracentrifugation of the latent ATPase gave a MW of 400,000. The ATPase contained 5 different subunits .alpha., .beta., .gamma., .delta. and .epsilon. and their MW determined by SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis were 60,000, 54,000, 37,000, 27,000 and 9000, respectively. The subunit composition was determined with 14C-labeled, f1-ATPase prepared from cells grown on medium containing [U-14C]-labeled algal protein hydrolysate. Within the limitations of this method the results tentatively suggest a subunit composition of 3:3:1:1:3.
Isolation of ATPase from rat liver submitochondrial particles by chloroform treatment requires the presence of ATP or ADP during enzyme solubilization. In the absence of adenine nucleotides the enzyme activity is very...
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Isolation of ATPase from rat liver submitochondrial particles by chloroform treatment requires the presence of ATP or ADP during enzyme solubilization. In the absence of adenine nucleotides the enzyme activity is very low although all protein components off1-ATPase are released. The low concentrations of ATP or ADP required (5 .mu.M) indicate that the high affinity nucleotide-binding sites are involved in enzyme stabilization. Other nucleotides tested (ITP, GTP, UTP, CTP) were less effective. Polyacrylamide gel electrophoresis and immunodiffusion in agar plates revealed that in the absence of adenine nucleotides a fraction off1-ATPase released by chloroform treatment is split into fragments. The part of the dissociated enzyme molecule has a MW identical with that of a .beta.-subunit off1-ATPase. Dissociation of the f1-ATPase molecule was prevented by aurovertin. Crude f1-ATPase solubilized by chloroform treatment was further purified by Sepharose 6B gel filtration. Specific ATPase activity of the purified enzyme was 90 .*** Pi/min per mg protein and the enzyme was composed of 5 protein subunits (.alpha., .beta., .gamma., .delta., .epsilon.) and MW 58,000, 55,000, 28,000, 13,000 and 8000, respectively. Chloroform-released f1-ATPase from rat liver mitochondria displayed immunochemical cross-reactivity with that isolated from beef heart mitochondria.
The abdominal aortas and right coronary arteries removed during autopsies were gathered from over 18,000 subjects in 19 location-race groups. Sudan-stained intimal surfaces were graded for the percent as raised lesion...
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The abdominal aortas and right coronary arteries removed during autopsies were gathered from over 18,000 subjects in 19 location-race groups. Sudan-stained intimal surfaces were graded for the percent as raised lesions (R) and fatty streaks (f). The proportions of all types of lesions (ATL = f + R) that were raised (RaL = R .div. ATL) were studied. The difference between the observed RaL (in subjects having atherosclerosis-related conditions) and the expected RaL (in age-, sex- and ATL-matched subjects without such conditions) measured the excess of RaL, which by inference indicated the tendency for an excess of raised lesions to be produced in place offatty streaks. In cases of coronary heart disease (CHD), a large excess of RaL was found consistently on the average. The coronary arteries and aortas of hypertensive subjects, compared with those of nonhypertensives, had a small and inconsistent excess of RaL. Both CHD and hypertension were characterized by a marked tendency for severe involvement by ATL, including extensive fatty streaks, leaving only small remnants of normal intima. Some factors (Class A) act to form fatty streaks and also to continue advancing them into raised lesions. Once the fatty streaks are formed, some new factors (Class B2) convert them into raised lesions. Apparently hypertension is a Class A type of atherogenic agent, and CHD is promoted by exceptionally strong effects of both A and B2 types of causation. If the assumptions of the model are true, then some of the more important causes of atherosclerosis (Class B causes) begin to act only after the fatty streaks have formed.
Aurovertin forms a complex with soluble beef heart mitochondrial ATPase (f 1 ) while exhibiting a biphasic fluorence enhancement. The effect of substrate, activators and inhibitors off 1 1 of the fluorescence of the ...
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Aurovertin forms a complex with soluble beef heart mitochondrial ATPase (f 1 ) while exhibiting a biphasic fluorence enhancement. The effect of substrate, activators and inhibitors off 1 1 of the fluorescence of the aurovertin-f 1 complex is reported. The aurovertin-f 1 complex can exist in two different states, one showing low fluorescence and the other with high fluorescence. Transition into the low fluorescence state is induced by various nucleoside triphosphates (ATP ± Mg 2+ , ITP ± Mg 2+ , GIP + Gg 2+ , and AMP-P(NH)P ± Mg 2+ ). The rate and extent offluorescence decrease caused by nucleotide addition (except that caused by ATP) is dependent on the presence of added Mg 2+ . The inhibitors of ATPase activity (AMP-P(NH)P, GMP-P(NH)P and EDTA) at concentrations that inhibit hydrolysis of ATP did not prevent the ATP induced decrease of aurovertin fluorescence. EDTA at high concentration (>0.4 mM) enhanced the effect of ADP. The complex of aurovertin with f 1 that had previously been treated with butanedione loses sensitivity to ATP. Addition of ADP to the system containing butanedione-treated enzyme caused a 2-fold greater enhancement offluorescence than the addition of ADP to the control system. In contrast to the butanedione-treated enzyme, the complex of aurovertin with f 1 previously treated at pH 5.6 loses sensitivity to ADP. Addition of ATP to this system lowered the fluorescence as in the system containing native enzyme. On the basis of the analyses of the aurovertin fluorescence changes and hydrolytic activity off 1 , the existence of several types of ligand binding sties with varying degrees of specificity are proposed. It is further proposed that these sites are important in control of the conformation and the catalytic properties of the ATPase molecule.
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