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Acta biochimica et biophysica Hungarica最新文献

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The first two years of the Latin American School of Biophysics sponsored by IUPAB--a prospective view. 由IUPAB赞助的拉丁美洲生物物理学院的前两年——一个前瞻性的观点。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
S Estrada
{"title":"The first two years of the Latin American School of Biophysics sponsored by IUPAB--a prospective view.","authors":"S Estrada","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 3-4","pages":"183-8"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13291150","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The effect of membrane potential on the limited tryptic digestion of the sarcoplasmic reticulum Ca(2+)-ATPase. 膜电位对肌浆网Ca(2+)- atp酶有限胰酶消化的影响。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
L Veres, I Szabó, L Dux
{"title":"The effect of membrane potential on the limited tryptic digestion of the sarcoplasmic reticulum Ca(2+)-ATPase.","authors":"L Veres,&nbsp;I Szabó,&nbsp;L Dux","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The tryptic cleavage process of the sarcoplasmic reticulum Ca(2+)-ATPase was analysed under the influence of experimentally generated membrane potential. The digestion of the Ca2+ transport enzyme was stopped before the dissipation of the potential response. The cleavage products reflected the actual conformation of the enzyme as the low Ca2+ affinity E2, under the influence of inside positive, and as the high Ca2+ affinity E1 conformation under the influence of inside negative potential. These results provide further support for the possible role of transient membrane potential changes in the regulation of the conformational equilibrium of the sarcoplasmic reticulum Ca2+ pump enzyme.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"17-23"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Rec mutants of Escherichia coli deficient in subunits of rec BC (D) complex. 大肠杆菌Rec突变体缺乏Rec BC (D)复合物亚基。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
E Tenke, G Bánfalvi
{"title":"Rec mutants of Escherichia coli deficient in subunits of rec BC (D) complex.","authors":"E Tenke,&nbsp;G Bánfalvi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The inactivation of rec BC (D) DNase upon chromatography on DEAE-cellulose was observed. Simultaneously DNA-stimulated ATPases (I and II) and DNase activities on single- and double-stranded DNA substrates were measured in Escherichia coli rec+ and rec- cell extracts. Normal levels of ATPase I and II were detected in rec+ cells. Rec A- cells were lacking DNA dependent ATPase I, while rec B single and rec BC double mutants were defective in DNA dependent ATPase II, the second major enzyme of this type. Rec B and C mutations did not change DNase activities. Rec A mutation significantly increased DNase activity on linear single-stranded substrate.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"101-9"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125059","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Enzymatic properties, metal composition and SH-group reactivity of fragmented sarcoplasmic reticulum isolated from rabbit skeletal muscle. 兔骨骼肌肌浆网碎片的酶学性质、金属组成和sh -基团反应性。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
M Szabolcs
{"title":"Enzymatic properties, metal composition and SH-group reactivity of fragmented sarcoplasmic reticulum isolated from rabbit skeletal muscle.","authors":"M Szabolcs","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Comparison of properties of fragmented sarcoplasmic reticulum samples isolated by several methods is reported. It was found that the protein composition does not differ significantly in samples which were or were not washed with 0.6 M KCl when isolated. In the case of samples washed with KCl solution the Zn concentration, the Ca/Mg ratio (determined from experimental data), acetylcholinesterase and superoxide dismutase activities were higher whereas Ca+Mg-activated ATPase and p-nitrophenylphosphatase activities were lower than those of samples which were not washed with 0.6 M KCl. In the latter samples the amount of SH-groups and the reactivity of fast SH-s are higher in Ca+EGTA containing media than in media containing only EGTA. In contrast in the case of samples washed with KCl solution the results are the opposite. In conclusion, washing of FSR with 0.6 M KCl alters the metal composition, enzymatic properties, SH-group reactivity and as a result of these probably the conformation of the protein samples, as well.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"111-24"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125061","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Inhibition of cytochrome C oxidase by glutathione in vitro. 谷胱甘肽对细胞色素C氧化酶的体外抑制作用。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
G Gullner
{"title":"Inhibition of cytochrome C oxidase by glutathione in vitro.","authors":"G Gullner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"31-5"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13125062","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Analysis of the proteolytic degradation products of hyaline cartilage proteoglycans. 透明软骨蛋白聚糖的蛋白水解降解产物分析。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
F Liszt, K Schnittker-Schulze, H W Stuhlsatz, H Greiling
{"title":"Analysis of the proteolytic degradation products of hyaline cartilage proteoglycans.","authors":"F Liszt,&nbsp;K Schnittker-Schulze,&nbsp;H W Stuhlsatz,&nbsp;H Greiling","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The proteolytic degradation products of nasal hyaline cartilage proteoglycans produced by polymorphonuclear leukocyte lysosomal enzymes were investigated. The protein content of the degradation products is 7.0-8.6% corresponding to a peptide chain of 24-28 amino acids and the relative molecular mass of the total fragment is M(r) = 37,600-39,200. On an average, each proteoglycan fragment contains two chondroitin-sulphate chains (M(r) = 22,000-22,400), every fourth fragment contains a keratan sulphate chain (M(r) = 7000-7200) and every seventh to eighth contains an O-glycosidic oligosaccharide. The results of the disaccharide analysis show that the galactosaminoglycan chains contain 76.2-83.6% chondroitin-4-sulphate, 12.9-19.4% chondroitin-6-sulphate, 3.5-3.8% chondroitin and no dermatan sulphate. Since composition and relative molecular mass of the chondroitin sulphate and keratan sulphate chains from the degradation products resemble those from native proteoglycans, it is suggested that the degradation of the proteoglycans occurs by proteinases that attack preferably the chondroitin sulphate region of the core protein.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 3-4","pages":"147-55"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12890639","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Effect of phospholipids on thyroid 5'-nucleotidase. 磷脂对甲状腺5′-核苷酸酶的影响。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
J Niedzwiecka, L Jaroszewicz
{"title":"Effect of phospholipids on thyroid 5'-nucleotidase.","authors":"J Niedzwiecka,&nbsp;L Jaroszewicz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Phospholipids were separated from 5'-nucleotidase in thyroid plasma membranes by Sephadex G-200 gel filtration. After removal of lipids 5'-nucleotidase was still active and reassociation of the enzyme with phospholipids had a little effect on the increase of enzyme activity. Arrhenius plot of the 5'-nucleotidase activity in native thyroid plasma membranes clearly exhibited a break at 28 degrees C. Biphasic nature of Arrhenius plot showed that the enzyme activity was influenced by physical state of membrane bilayer, although phospholipids were not obligatory cofactor for this enzyme.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"47-56"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13285641","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Fast components of the absorption changes of bacteriorhodopsin at 275 nm and 296 nm. 细菌紫质在275 nm和296 nm吸收变化的快速组分。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
S Stoylova, R Tóth-Boconádi, L Keszthelyi
{"title":"Fast components of the absorption changes of bacteriorhodopsin at 275 nm and 296 nm.","authors":"S Stoylova,&nbsp;R Tóth-Boconádi,&nbsp;L Keszthelyi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A very fast component (life time 0.2 microsecond) was found in the flash-induced absorption changes of bacteriorhodopsin (bR) at 275 nm and 296 nm. This result was obtained by measuring the absorption changes at well defined delay times after the exciting laser flash (590 nm, 20 ns pulse duration). For this purpose a second laser flash was used as the monitoring beam. The very fast absorption changes of bR in the UV range are due to the rapid perturbation of the opsin moiety near the chromophore, as a result of the all-trans to 13-cis isomerization of the retinal taking place on the same time scale.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 3-4","pages":"139-45"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13291234","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Effects of polyethylene terephthalate on yeast alcohol dehydrogenase. 聚对苯二甲酸乙二醇酯对酵母醇脱氢酶的影响。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
L M Simon, K Heinrichova, I Veszelka, B Szajáni
{"title":"Effects of polyethylene terephthalate on yeast alcohol dehydrogenase.","authors":"L M Simon,&nbsp;K Heinrichova,&nbsp;I Veszelka,&nbsp;B Szajáni","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Yeast alcohol dehydrogenase (alcohol: NAD+ oxidoreductase, EC 1.1.1.1) was adsorbed onto polyethylene terephthalate, a synthetic polymer. The effects of the polymer on the properties of the enzyme were studied. The specific activity of the bound enzyme on protein basis was only 1.2 per cent of the specific activity of the soluble enzyme. The optimum pH for the catalytic activity was strongly shifted toward acidic direction. The apparent temperature optimum of the bound enzyme was identical with that of the soluble form. The apparent Michaelis constants of the bound enzyme were higher for both ethanol and NAD+. The conformational stability of the enzyme against heat treatment and urea was decreased as a consequence of adsorption.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13305584","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin. 能够裂解胰蛋白酶活性位点滴定物作为底物的酶是一种具有类似白蛋白的电泳流动性的羧酸酯酶。
Acta biochimica et biophysica Hungarica Pub Date : 1990-01-01
J Tözsér, T M Marsalkó, M Punyiczki, P Elödi
{"title":"The enzyme capable to cleave trypsin active site titrant as substrate is a carboxylesterase with electrophoretic mobility similar to albumin.","authors":"J Tözsér,&nbsp;T M Marsalkó,&nbsp;M Punyiczki,&nbsp;P Elödi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>An enzyme isolated from Ehrlich ascites plasma and capable of cleaving trypsin active site titrant 4-nitrophenyl-p-guanidinobenzoate (Steven, F.S. and Al-Achmad, R.K. (1983) has been further investigated. The substrate hydrolysis follows Michaelis-Menten kinetics. The molecular mass of the enzyme is 50-70 kDa by gel filtration and SDS polyacrylamide gel electrophoresis. It has the mobility of albumin and coelutes with a carboxylesterase activity on a cation exchange column. (Cbz-Arg-NH)2-Rhodamine, the specific noncompetitive inhibitor of guanidinobenzoatase, also inhibits the carboxylesterase activity. Therefore, the guanidinobenzoatase activity of Ehrlich ascites plasma is a carboxylesterase (EC 3.1.1.1.) which likely originates from blood.</p>","PeriodicalId":77479,"journal":{"name":"Acta biochimica et biophysica Hungarica","volume":"25 1-2","pages":"57-65"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13285642","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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