Hoppe-Seyler's Zeitschrift fur physiologische Chemie最新文献_第9页

The isolation of lysosomes from normal rat liver by affinity chromatography. 亲和层析法分离正常大鼠肝脏溶酶体。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01 DOI: 10.1515/bchm2.1984.365.1.539

F J Kamrath, G Dodt, H Debuch, G Uhlenbruck

引用次数: 10

Purification and properties of a manganese-containing superoxide dismutase from Acholeplasma laidlawii. 一种含锰超氧化物歧化酶的纯化及性质研究。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01 DOI: 10.1515/bchm2.1984.365.1.577

R Reinards, R Altdorf, H D Ohlenbusch

引用次数: 4

Slow migrating proteinase inhibitors in human serum. 人血清中缓慢迁移的蛋白酶抑制剂。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01

L Odum

引用次数: 0

[Mechanism of action of silibinin. V. Effect of silibinin on the synthesis of ribosomal RNA, mRNA and tRNA in rat liver in vivo]. 水飞蓟宾的作用机理。五、水飞蓟宾对体内大鼠肝脏核糖体RNA、mRNA和tRNA合成的影响。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01

J Sonnenbichler, I Zetl

引用次数: 0

Low molecular mass bronchial proteinase inhibitor and alpha 1-proteinase inhibitor in sputum and bronchoalveolar lavage. 痰液和支气管肺泡灌洗液中低分子质量支气管蛋白酶抑制剂和α 1蛋白酶抑制剂。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01 DOI: 10.1515/bchm2.1984.365.1.587

R A Stockley, H M Morrison, S Smith, T Tetley

{"title":"Low molecular mass bronchial proteinase inhibitor and alpha 1-proteinase inhibitor in sputum and bronchoalveolar lavage.","authors":"R A Stockley, H M Morrison, S Smith, T Tetley","doi":"10.1515/bchm2.1984.365.1.587","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.587","url":null,"abstract":"The concentration of a low molecular mass bronchial mucus inhibitor of proteolytic enzymes (BMPI) was measured in lung secretions from patients with chronic bronchitis and compared to the concentrations of albumin and alpha 1-proteinase inhibitor (alpha 1-PI). The concentration of all three proteins was lower in bronchoalveolar lavage samples than in sputum obtained from the same patient. However the relationship between the proteins (concentrations relative to each other) was similar in both secretions suggesting the differences in concentrations were only dilutional. The molar concentration of BMPI in both secretions was generally greater than that of alpha 1-PI suggesting that most of the anti-elastase screen (congruent to 75%) was due to the former protein. Furthermore inhibitory studies using both purified leukocyte elastase and porcine pancreatic elastase show that the inhibitory capacity of lung alpha 1-PI varied and accounted for about 16% of the total inhibition of leukocyte elastase in sputum. However, the inhibitory function of alpha 1-PI was less in bronchoalveolar lavage fluids compared to sputum (p less than 0.05) and accounted for about 5% of the total inhibitory capacity for leukocyte elastase. It is concluded that alpha 1-PI contributes only a part of the anti-elastase screen of secretions from patients with chronic bronchitis. Furthermore it is inactivated to a varying degree in most secretions and its remaining inhibitory capacity represents only a minor proportion of the total inhibitory capacity.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 5","pages":"587-95"},"PeriodicalIF":0.0,"publicationDate":"1984-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.587","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17392395","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: 35

The preparation of hydrophilic derivatives of band 3 protein by acylation of the human red blood cell membrane. 人红细胞膜酰化制备带3蛋白亲水性衍生物。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01 DOI: 10.1515/bchm2.1984.365.1.525

F Herbst, V Rudloff

引用次数: 1

Evidence for a cryptic lectin site in the cell-binding domain of plasma fibronectin. 血浆纤维连接蛋白的细胞结合区域有一个隐凝素位点的证据。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-05-01 DOI: 10.1515/bchm2.1984.365.1.517

H Hörmann, H Richter, V Jelinić

{"title":"Evidence for a cryptic lectin site in the cell-binding domain of plasma fibronectin.","authors":"H Hörmann, H Richter, V Jelinić","doi":"10.1515/bchm2.1984.365.1.517","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.517","url":null,"abstract":"Various proteolytic fragments from the central region of the fibronectin subunit chains containing the main cell-affinity site were applied in cell binding studies using peritoneal macrophages of guinea pigs. A 125I-labelled 23-kDa peptide was relatively well bound by the cells. Attachment to cells was partially inhibited by wheat germ lectin, suggesting a lectin-like site in the cell-binding domain which recognizes oligosaccharide groups with terminal N-acetylglucosamine or N-acetylneuraminic acid. Binding was inhibited by N-acetylneuraminic acid with half-maximal effect at 2 X 10(-3) M. Other inhibitors were a sialic acid rich ganglioside preparation and fetuin, a sialic acid-containing glycoprotein. In contrast to the 23-kDa peptide a 125I-labelled 125-kDa fragment was only weakly bound, although it included the sequence of the 23-kDa peptide on its C-terminus. The residual binding was weakly inhibited by low concentrations of wheat germ lectin and was remarkably improved by higher concentrations. The behavior of the peptide was explained by the presence of a sialic acid-containing oligosaccharide side chain localized outside of the 23-kDa region and interacting with the lectin-like site in the cell-binding sequence. In accord with this suggestion a 95-kDa fragment representing the oligosaccharide-containing part of the 125-kDa peptide was capable of inhibiting at least partially the cell attachment of the 23-kDa piece. The results indicate a lectin-like affinity site in the cell-binding region of fibronectin which is accessible in the 23-kDa peptide, but is masked in the 125-kDa fragment and in fibronectin by a sialic acid-containing oligosaccharide moiety.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 5","pages":"517-24"},"PeriodicalIF":0.0,"publicationDate":"1984-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.517","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17155745","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: 11

The biological potency of covalent insulin-receptor complexes. Dependence on site of cross-linkage. 共价胰岛素受体复合物的生物学效力。交联位点依赖性。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.493

G Klotz, D J Saunders, D Brandenburg

{"title":"The biological potency of covalent insulin-receptor complexes. Dependence on site of cross-linkage.","authors":"G Klotz, D J Saunders, D Brandenburg","doi":"10.1515/bchm2.1984.365.1.493","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.493","url":null,"abstract":"A radioactive photosensitive insulin analogue, 125I-N epsilon B29-(4-azido-2-nitrophenyl-acetyl)insulin, was covalently bound to the receptors of isolated rat adipocytes by irradiation with UV light. This caused a stimulation of lipogenesis. The relative potency of the covalent complexes to that of normal reversible complexes was calculated by comparing the amounts of radioactivity required to be covalently or reversibly bound by adipocytes to cause the same levels of stimulation. For several different occupancies , this relative potency was constant at 50 +/- 3%. Previous studies had shown that the relative potency of covalently bound 125I-N alpha B2-(4-azido-2- nitrophenylacetyl )des- PheB1 -insulin was only 25 +/- 4% under identical conditions. This demonstrates that the sites of crosslinking have a marked effect on the potency of the covalent hormone-receptor complex. It appears that attachment through the C-terminus of the B-chain leads to a better stabilization of the biologically active form than linking through the more flexible N-terminus.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 4","pages":"493-8"},"PeriodicalIF":0.0,"publicationDate":"1984-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.493","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17436150","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: 4

Qualitative studies of lung lavage alpha 1-proteinase inhibitor. 肺灌洗α 1蛋白酶抑制剂的定性研究。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.503

R A Stockley, S C Afford

引用次数: 25

Characterization of proteoglycans synthesized by cultured arterial smooth muscle cells of the rat. 培养大鼠动脉平滑肌细胞合成蛋白聚糖的表征。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.445

A Schmidt, A von Teutul, E Buddecke

{"title":"Characterization of proteoglycans synthesized by cultured arterial smooth muscle cells of the rat.","authors":"A Schmidt, A von Teutul, E Buddecke","doi":"10.1515/bchm2.1984.365.1.445","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.445","url":null,"abstract":"Arterial smooth muscle cells cultured from rat aorta were labelled with sodium [35S]-sulfate in combination with either [3H]glucosamine or [3H]mannose. The newly synthesized hyaluronate and sulfated proteoglycans obtained from the growth medium (M-PG) and extracted from the cell layer (C-PG) with 4M guanidinium chloride in the presence of proteinase inhibitors were purified by sequential fractionation on Sepharose 4B CL, equilibrium density gradient centrifugation and ion exchange chromatography under dissociative conditions. Gel filtration of M-PG resulted in the separation of free hyaluronate and two size classes of [35S]-proteoglycan populations eluted at Kav 0.15 (fraction M-A) and 0.48 (fraction M-B). On further fractionation M-A dissociated into hyaluronate (Mr 1.6 X 10(6)) and a proteoglycan monomer (M-PG A, Mr 180 000), which contained chondroitin 4-sulfate (Mr 21 000) as the main glycosaminoglycan moiety. The proteoglycan isolated from M-B (M-PG B) was identified as a proteoglycan monomer (Mr 200 000) containing mainly chondroitin sulfate/dermatan sulfate hybrid side chains (Mr 34 000). [3H]Mannose labelling and binding to ConA Sepharose of both M-PG A and B indicated the presence of oligosaccharides of the glycoprotein type. An analogous fractionation of proteoglycans associated with the cell layer yielded two hyaluronate-proteoglycan complexes (C- PreA and C-A). The proteoglycan monomers of these complexes (C-PG PreA and C-PG A) had Mr values of 420 000 and 130 000. A non-complexed proteoglycan monomer C-PG B (Mr 90 000) was also found. All cell layer bound proteoglycans had glycosaminoglycan side chains with Mr approximately 36 000 but the predominant glycosaminoglycan component was either heparan sulfate, chondroitin sulfate or dermatan sulfate. All cell layer bound proteoglycans contained [3H]mannose radioactivity, about 15% of which was bound to ConA Sepharose.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 4","pages":"445-56"},"PeriodicalIF":0.0,"publicationDate":"1984-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.445","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17788595","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: 16