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Query: UMLS:C0155339 (Brown)
 12,436 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The specific activity of cytochrome-oxidase, succinate-cytochrome c reductase and su-cinate-oxidase of brown adipose tissue mitochondria of 17-day-old rats was found to be twice as high in brwon adipose tissue mitochondria as in the liver. The specific activity of rotenone-sensitive NADH-cytochrome c reductase and NADH-oxidase was found to be six times higher in brown adipose tissue mitochondria than in the liver. 2. Brown adipose tissue mitochondria have extremely low activity of outer membrane enzymes. When compared with liver the specific activity of rotenone-insensitive NADH-cytochrome c reductase was found to be seven times lower, the specific activity of monoamineoxidase up to 30 times lower according to the substrate used. 3. The optimum conditions for the determination of both NADH-cytochrome c reductases in brown adipose tissue mitochondria were more specified on the base of the following findings: (a) the outer membrane rotenone-insensitive NADH-cytochrome c reductase is strongly inactivated by freezing-thawing, (b) freezing-thawing, alone is insufficient to release completely maximal activity of rotenone-sensitive NADH-cytochrone c reductase, freezing-thawing activite can be further potentiated by e.g. trypsin treatment. 4. The activities of the outer membranes of brown-adipose tissue mitochondria are discussed with regards to the structural integrity of the outer membrane, the activities of the inner membrane enzymes are discussed with regards to the functional specifity of the tissue.
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PMID:Activity of the inner and outer membrane oxidative enzymes in brown adipose tissue mitochondria. 16 30

Rat aortic smooth muscle cells in culture were incubated with rat or human iodinated low and high density lipoprotein at 5-50 mug/ml for 3 h. With the homologous lipoproteins, 25-49% of total cellular protein radioactivity was trypsin releasable and was considered as surface-bound radioactivity, while the balance represented cellular uptake. The ratio of surface-bound to cellular label was higher when the cells were incubated with human lipoproteins and was about 9 : 1 with human high density lipoprotein. Cellular uptake of rat low density lipoprotein was about twice that of rat high density lipoprotein, while degradation of labeled protein, which had presumably followed protein uptake, was similar and ranged from 20 to 25% of protein uptake in 3 h. Experiments designed to test the effect of cell density on lipoprotein uptake have shown that the uptake was related inversely to cell density. Thus, the lower lipoprotein uptake encountered in the rat smooth muscle cells, compared to that described for human fibroblasts (Goldstein, J.L. and Brown, M.S. (1974) J. Biol. Chem. 249, 5153-5162), could be due in part to the much lower cell density used in the latter studies, as well as to cell type and species difference.
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PMID:Surface binding and interiorization of homologous and heterologous serum lipoproteins by rat aortic smooth muscle cells in culture. 16

Several fragments of bovine serum albumin have been isolated following limited tryptic hydrolysis and their positions then determined in the bovine serum albumin sequence published by J. R. Brown ((1975), Fed. Proc., Fed. Am. Soc. Exp. Biol. 34, 591). When bovine serum albumin was coupled to palmityl-aminoethylamino-agarose and digested with trypsin, two fragments were obtained: (a) peptide 115-184, containing the highly aromatic disulfide loop 3 of Brown's model, and (b) a larger fragment, residues 377-581, containing disulfide loops 7-9. This fragment constitutes the third of the three domains of the albumin molecule. From bovine serum albumin digested in solution, peptide 115-184 was again obtained, as well as (c) a 39,000-dalton fragment identified as residues 198-581, loops 4-9 of the second and third domains, but with a long, tryptophan-containing segment 204-238 missing from loop 4. The ability to isolate these fragments without cleaving disulfide bridges is partial confirmation of the proposed model of bovine serum albumin as a series of nine independent loops.
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PMID:Fragments of bovine serum albumin produced by limited proteolysis. Isolation and characterization of tryptic fragments. 109 43

Sindbis virus is a membrane-containing virus which has two glycoproteins organized in an icosahedral lattice. Protein-protein associations have been identified which participate in the formation of the icosahedron and these associations are stabilized by intramolecular disulfide bridges (Anthony, R. P., and Brown, D. T., 1990, J. Virol. 65, 1187-1194). The present study further examines the role of disulfides in the structure and function of Sindbis virus by following the effect of dithiothreitol on the protease sensitivity of envelope proteins as well as the electron microscopic appearance and infectivity of Sindbis virus. Treatment of isolated virus with 5 mM dithiothreitol for 6 hr causes a marked increase in trypsin sensitivity of both E1 and E2, profound morphological alterations in the viral envelope, increased susceptibility of the nucleocapsid to RNase, and 95% loss of infectivity. These effects are greatly enhanced and accelerated when treatment with DTT is preceded by a brief exposure of the virus to pH 5.3, suggesting that acid-induced conformational changes render structurally critical disulfides more accessible to reductive cleavage by DTT. When compared to other manipulations known to change the conformation of the viral envelope, such as heating to 51 or 60 degrees or exposure to acid pH, only the exposure to DTT with or without prior acid treatment caused marked structural changes correlated with a loss of infectivity. These data provide electron microscopic and functional evidence that intact disulfide bonds are critical for the stability of the virus envelope and suggest that the cleavage of critical disulfide(s) may play a role in the process of virus infection.
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PMID:Disulfide bonds are essential for the stability of the Sindbis virus envelope. 152 37

Rupture of the internal elastic lamina may occur spontaneously with age in certain arteries of the rat and to various extents in different strains. This phenomenon may have some bearing on certain aspects of arterial pathology. For this study, we investigated biochemically the mechanisms of formation of interruptions in the internal elastic lamina (IIEL) by comparing aortas of Brown Norway (BN) rats, which develop numerous IIEL in the abdominal aorta, with those of Long-Evans (LE) rats, which develop none. We isolated aortic elastin from BN and LE rats and determined its amino acid composition and its susceptibility to different elastases. No differences were found between the two strains, but the quantity of elastin isolated per aorta was lower in the BN than in the LE rats. Elastase-like activity (ELA) of whole aortic extracts, measured with Suc(Ala)3NA as a substrate, was greater in the BN rats than in the LE rats of both sexes. The assay of ELA in endothelium, media, and adventitia extracted separately showed very low levels in the media compared to the endothelium and adventitia. The endothelium accounts for about one-half of the total aortic ELA, but a difference between the two strains was detected only in the adventitia. With 3H-insoluble elastins prepared from BN and LE aortas as substrates, elastinolytic activity (EA) was detected only in extracts of endothelium after prior exposure to trypsin. Extracts from BN endothelium on BN elastin were more active than were those from LE endothelium on LE elastin. The assay of lysyl oxidase activity in aortic extracts from the two strains with 3H-collagen from chick embryo calvaria as the substrate showed a lower activity in the BN than in the LE rats. Taken together, these results suggest that increased elastase activity and decreased lysyl oxidase activity may be involved in the formation of IIEL.
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PMID:Role of elastase and lysyl oxidase activity in spontaneous rupture of internal elastic lamina in rats. 197 75

Immunopathogenicity of trypsin-solubilized or non-solubilized renal tubular basement membrane (TBM) of the Lewis (LEW) rat was investigated. Autoimmune tubulointerstitial nephritis (TIN) was induced in BALB/c mice by immunization with trypsin-solubilized LEW rat TBM, while immunization with non-solubilized TBM did not produce the disease. Based on this preliminary experiment we studied the characterization of immunogenic and nephritogenic TBM antigen of the LEW rat. TIN was characterized by severe mononuclear cell infiltrates with multi-nucleated giant cells in the interstitium, tubular destruction and intensive IgG and C3 deposits along the TBM. Anti-TBM antisera and eluate from the nephritic mouse kidneys reacted with the TBM of normal LEW rat kidney by immunofluorescence. LEW rat TBM was also detected immunofluorescently by using antisera from BALB/c mice immunized with autologous trypsin-solubilized TBM. A competitive inhibition test revealed a higher titer of anti-TBM antibody in the eluate than in the adsorption-treated antisera per microgram IgG. Immunoblotting showed one reactive band with a molecular weight of 45,000 daltons, and the blotting patterns in tryptic TBM of the Brown Norway (BN) and LEW rats appeared similar. Amino acid analysis of nephritogenic LEW rat tryptic TBM showed that it contained no hydroxyproline and hydroxylysine, suggesting that this TBM preparation was not collagenous. These findings suggest that tryptic digestion contributes to the release of nephritogenic antigen from the LEW rat TBM and that this antigen system might participate in the immune system involved in the anti-TBM associated TIN that is well known to be induced by non-digested TBM of TBM antigen positive animals.
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PMID:Detection of nephritogenic antigen from the Lewis rat renal tubular basement membrane. 218 35

We examined whether Brown Norway rat plasma (BN/May Pfd f) contains alpha 1-cysteine proteinase inhibitor (alpha 1-CPI), also called major acute phase alpha 1-protein or T-kininogen. T-kininogen is a low molecular weight kininogen from which kinin can be released by trypsin but not by kallikreins. The BN plasma reacted with rabbit anti-alpha 1-CPI gamma globulins. Purified alpha 1-CPI released a kinin-like activity with trypsin and with homogenate of salivary glands, as Brown Norway rat plasma did. High concentration of added rat urine induced a small release (10%) of kinin from alpha 1-CPI. Preincubation of Brown Norway rat plasma with rabbit anti-rat alpha 1-CPI gamma-globulins nearly suppressed the kinin-forming substrate of trypsin in this plasma. These results indicated that plasma of our Brown Norway rats contains only alpha 1-CPI as kinin-forming substrate. This plasma contains low amount of alpha 2-macroglobulin, while its content in orosomucoid and haptoglobin was a little larger than that of Wistar rat plasma.
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PMID:Acute phase plasma proteins in kininogen-deficient Brown Norway rats. 243 May 37

Mutations in the plasma membrane H(+)-ATPase gene (PMA1) of Saccharomyces cerevisiae that confer growth resistance to hygromycin B have been shown recently to cause a marked depolarization of whole cell membrane potential (Perlin, D. S., Brown, C. L., and Haber, J. E. (1988) J. Biol. Chem. 263, 18118-18122). In this report, the biochemical and genetic properties of H+-ATPases from four prominent hygromycin B-resistant pma1 mutants, pma1-105, pma1-114, pma1-147, and pma1-155, are described. Single base pair changes were identified in pma1-105, pma1-114, and pma1-147 that resulted in amino acid substitutions of Ser-368----Phe, Gly-158----Asp, Pro-640----Leu, respectively. An A----G transition mutation at -39 in the 5'-untranslated region of the mRNA of pma1-155 was also found. This mutation creates an out-of-Frame upstream AUG initiation codon that apparently reduces normal translation of PMA1. DNA sequence analysis of PMA1 from strain Y55 identified 9 base pair substitutions that resulted in 6 amino acid changes in nonconserved regions when compared to the published sequence for strain S288C. Plasma membranes of three of the four pma1 mutants contained normal amounts of H(+)-ATPase; membranes from pma1-155 contained enzyme at 62% of the wild-type level. The kinetics of ATP hydrolysis were most strongly altered for enzymes from pma1-105 and pma1-147 which showed changes in both Km and Vmax. A striking pH dependence for these parameters was found for enzyme from pma1-105 which resulted in a precipitous decline in Km and Vmax below pH 6.5. ATP hydrolysis by enzymes from pma1-105 and pma1-147 was insensitive to inhibition by vanadate. These enzymes, in contrast to wild-type and vanadate-sensitive mutant enzymes, were poorly protected from trypsin-induced inactivation by MgATP and vanadate or Pi alone. These results are pertinent to the mechanism of vanadate-induced enzyme inhibition and suggest that Ser-368 and Pro-640 influence the affinity of the phosphate-binding site for Pi. All mutant enzymes catalyzed ATP-induced pH gradient formation following purification and reconstitution into liposomes. Finally, these results further demonstrate the usefulness of hygromycin B as a generalized screening tool for isolating diverse plasma membrane ATPase mutants.
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PMID:Defective H(+)-ATPase of hygromycin B-resistant pma1 mutants fromSaccharomyces cerevisiae. 253 14

A direct radioimmunoassay (RIA) for rat high molecular weight kininogen (HMW Kg) was developed that enabled us to detect 71 fmol/ml of HMW Kg. The antibodies did not crossreact in the RIA with up to 5 nmol of purified rat alpha 1 cysteine proteinase inhibitor (T-kininogen). When various quantities of pure HMW Kg were either quantified by the RIA or by the measurement of kinin contents determined after trypsin hydrolysis, identical values were obtained by both methods. This RIA allowed the measurement of HMW Kg in 0.015 to 1 microliter of rat plasma. HMW Kg levels in plasma of Wistar rats and in Brown Norway rats of the Orlean Strain (BN/Orl) were 1.52 +/- 0.05 (n = 6) and 2.050 +/- 0.015 (n = 8) nmol/ml respectively. In the Brown Norway rats of the Katholiek strain (BN/Kat) that are considered to be deficient in HMW Kg, immunoreactive HMW Kg levels were less than 2% of those of the BN/Orl rats. These results confirm that the BN/Kat animals have a molecular defect in HMW Kg.
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PMID:Direct radioimmunoassay for rat high molecular weight kininogen. Measurement of immunoreactive high molecular weight kininogen in normal and kininogen deficient plasma. 348 Dec 12

Bovine adrenal cortex contains a high molecular weight casein kinase II-like enzyme (Mr 500,000) that phosphorylates a specific serine residue in the cytoplasmic domain of the low density lipoprotein (LDL) receptor (Kishimoto, A., Brown, M. S., Slaughter, C. A., and Goldstein, J. L. (1987) J Biol. Chem. 262, 1344-1351). In the current paper, we provide evidence to suggest that this 500-kDa kinase can be dissociated into two subunits, a catalytic subunit and an activator subunit, by treatment with 1 M NaCl. The catalytic subunit was purified to homogeneity (greater than 100,000-fold) using affinity chromatography on GTP-agarose plus several other chromatography steps. It had an Mr of 50,000 by gel filtration and 35,000 by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The catalytic subunit phosphorylated casein actively, but it phosphorylated the LDL receptor with only low affinity. The affinity for the LDL receptor was increased 10-fold (saturation at 10 nM LDL receptor) by addition of a second protein that was released from a high molecular weight 500-kDa complex by 1 M NaCl. This activator protein (Mr 120,000 by gel filtration) was extremely heat stable but was destroyed by trypsin. It appeared to be required in stoichiometric amounts with relation to the LDL receptor. It did not increase the ability of the 50-kDa subunit to phosphorylate casein nor did it activate phosphorylation of the LDL receptor or casein by classic casein kinase II. The current data raise the possibility that the specificity of the 500-kDa LDL receptor kinase is attributable to a heat-stable activator subunit that binds to the LDL receptor and thereby renders it a better substrate for the catalytic subunit of the kinase.
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PMID:Purification of catalytic subunit of low density lipoprotein receptor kinase and identification of heat-stable activator protein. 359 14


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