Hoppe-Seyler's Zeitschrift fur physiologische Chemie最新文献_第5页

[Perissodactyla: the primary structure of hemoglobins from the lowland tapir (Tapirus terrestris): glutamic acid in position 2 of the beta chains]. [低地貘(Tapirus terrestris)血红蛋白的初级结构:β链2位的谷氨酸]。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-09-01

G Mazur, G Braunitzer

{"title":"[Perissodactyla: the primary structure of hemoglobins from the lowland tapir (Tapirus terrestris): glutamic acid in position 2 of the beta chains].","authors":"G Mazur, G Braunitzer","doi":"","DOIUrl":"","url":null,"abstract":"The hemoglobins from a lowland tapir (Tapirus terrestris) were analysed and the complete primary structure is described. The globin chains were separated on CM cellulose column in 8M urea and the amino-acid sequences were determined in the liquid phase sequenator. The results show that globin consists of two alpha chains (alpha I and alpha II) and beta major and beta minor components. The alpha chains differ only at one position: alpha I contains aspartic acid and alpha II glycine. The beta chains are heterogeneous: aspartic and glutamic acid were found at position beta 21 and beta 73 of the beta major components and asparagine and serine at position beta 139. In the beta minor components four positions were found with more than one amino acid, namely beta 2, beta 4, beta 6 and beta 56. The sequences are compared with those of man, horse and rhinoceros. Four residues of horse methemoglobin, which are involved in the alpha 1 beta 1 contacts are substituted in tapir hemoglobins. In the alpha chains: alpha 107(G14)Ser----Val, alpha 111-(G18) Val----Leu, alpha 115(GH3) Asn----Asp or Gly; in the beta chains: beta 116(G18) Arg----Gln. The amino acid at beta 2 of the major components is glutamic acid while glutamine and histidine are found in the minor components. Although glutamic acid, a binding site for ATP, does not interact with 2,3-bisphosphoglycerate, glutamine and histidine in the minor components are responsible for the slight effect of 2,3-bisphosphoglycerate on tapir hemoglobin.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 9","pages":"1097-106"},"PeriodicalIF":0.0,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17215883","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

Human placental steroid-sulfatase solubilized with a cholic-acid derivative: molecular mass, kinetic properties and susceptibility to glycosidases. 用胆酸衍生物溶解的人胎盘类固醇硫酸酯酶:分子质量、动力学性质和对糖苷酶的敏感性。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-09-01 DOI: 10.1515/bchm2.1984.365.2.1145

L Dibbelt, E Kuss

{"title":"Human placental steroid-sulfatase solubilized with a cholic-acid derivative: molecular mass, kinetic properties and susceptibility to glycosidases.","authors":"L Dibbelt, E Kuss","doi":"10.1515/bchm2.1984.365.2.1145","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1145","url":null,"abstract":"Human placental steroid-sulfatase was extracted nearly quantitatively from microsomes as well as from acetone dry powder of placenta homogenates using CHAPS as detergent. The solubilized enzyme was enriched 10-fold by ammonium sulfate precipitation and gel chromatography. The sulfatase extracted from both microsomes and acetone dry powder eluted as a single fraction on Sepharose 6B, but with different apparent molecular masses (390 and 270 kDa, respectively). Kinetic experiments with the sulfate esters of dehydroepiandrosterone, 16 alpha-hydroxydehydroepiandrosterone, estrone, and estriol as substrates or inhibitors indicated that the solubilized sulfatase was fully active. Both the particulate and the extracted enzyme showed higher affinities for the 16-unsubstituted than for the 16 alpha-hydroxylated substrates. Whereas a competitive inhibition was observed in mixed substrate incubations with dehydroepiandrosterone sulfate/16 alpha-hydroxydehydroepiandrosterone sulfate and estrone sulfate/estriol sulfate, diverse patterns of inhibition were obtained with dehydroepiandrosterone sulfate/estrone sulfate, depending on the sulfatase preparation used. However, evidence for the distinct nature of the steroid-sulfatase and the estrogen-sulfatase was not obtained. The membrane-bound, but not the solubilized enzyme was to a certain degree sensitive to lipase and acetone. The solubilized sulfatase strongly bound to ConA-Sepharose. This observation together with the elution by alpha-methyl mannoside were indicative of the presence of carbohydrates on the sulfatase. Since its enzymatic activity was markedly decreased by the effects of alpha-mannosidase and N-acetylglucosaminidase, a possible involvement of the carbohydrate moiety in the catalytic activity of the sulfatase might be considered.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 9","pages":"1145-53"},"PeriodicalIF":0.0,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1145","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17650741","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: 14

Hemoglobin of the adult white stork (Ciconia ciconia, ciconiiformes). The primary structure of alpha A- and beta-chains from the only present hemoglobin component. 成年白鹳(Ciconia Ciconia, ciconiformes)的血红蛋白。α - A链和β链的初级结构来自唯一存在的血红蛋白成分。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-09-01 DOI: 10.1515/bchm2.1984.365.2.1107

J Godovac-Zimmermann, G Braunitzer

{"title":"Hemoglobin of the adult white stork (Ciconia ciconia, ciconiiformes). The primary structure of alpha A- and beta-chains from the only present hemoglobin component.","authors":"J Godovac-Zimmermann, G Braunitzer","doi":"10.1515/bchm2.1984.365.2.1107","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1107","url":null,"abstract":"The hemolysate obtained from erythrocytes of the adult White Stork (Ciconia ciconia) contains only one hemoglobin component, identified to be HbA. The complete primary structures of alpha A- and beta-chains are presented. The minor hemoglobin component HbD with alpha D-chains usually present in adult avian species was not detected by the White Stork. The sequence was determined by automatic Edman degradation of tryptic peptides and in the case of beta-chains additionally of the C-terminal peptide obtained by chemical cleavage at the Asp-Pro bond. Homologous comparison with the Greylag Goose (Anser anser) hemoglobin showed that the alpha A-chains differ by 23 amino-acid exchanges, the beta-chains by 17. Four of the substitutions in the alpha A-chains are in the alpha 1 beta 1-contact points, one in the alpha 1 beta 2-contacts and one in the amino acids near the heme. The amino-acid substitutions of the White Stork hemoglobin as compared to the other avian hemoglobins are discussed. We suggest that alpha D-chain is persistence of an embryonic gene.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 9","pages":"1107-13"},"PeriodicalIF":0.0,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1107","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17558470","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: 17

Bile secretion in hemoglobin-free perfused rat liver. 无血红蛋白灌注大鼠肝脏胆汁分泌。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-09-01 DOI: 10.1515/bchm2.1984.365.2.1115

H Krell, H Jäschke, H Höke, E Pfaff

引用次数: 16

Isolation of acid-resistant urinary trypsin inhibitors by high performance liquid chromatography and their characterization by N-terminal amino-acid sequence determination. 高效液相色谱法分离耐酸尿胰蛋白酶抑制剂及其n端氨基酸序列测定。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-09-01 DOI: 10.1515/bchm2.1984.365.2.1123

K Hochstrasser, P Reisinger, G J Albrecht, E Wachter, O L Schönberger

{"title":"Isolation of acid-resistant urinary trypsin inhibitors by high performance liquid chromatography and their characterization by N-terminal amino-acid sequence determination.","authors":"K Hochstrasser, P Reisinger, G J Albrecht, E Wachter, O L Schönberger","doi":"10.1515/bchm2.1984.365.2.1123","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1123","url":null,"abstract":"Two crude fractions of acid-resistant trypsin inhibitors (apparent molecular masses 44 and 20 kDa, respectively) were prepared from human urine by gel permeation chromatography. From both preparations the pure inhibitors were isolated by high performance liquid chromatography (HPLC). Their N-terminal amino-acid sequences were determined and compared with those of HI-30 and HI-14 as isolated by reversible binding to either immobilized trypsin or immobilized chymotrypsin. The N-terminal amino-acid sequence of the high-molecular mass inhibitor UI-I isolated by HPLC was identical with those of HI-30 and UI-C-I isolated via immobilized trypsin or chymotrypsin, respectively. The low-molecular mass inhibitors UI-II and UI-C-II differ from HI-14 by the N-terminal extension Glu-Val-Thr-Lys-when obtained by HPLC or by the extension Thr-Lys-when obtained via immobilized chymotrypsin, respectively. The comparison of these N-termini with the amino-acid sequence of HI-30 (Ala1-...-Val16-Thr-Glu-Val-Thr-Lys-HI-14) defines the low molecular urinary trypsin inhibitors as proteolytic degradation products of the high-molecular urinary inhibitor. Proteolysis may occur at different bonds. The existing discrepancies in molecular architecture and in molecular masses of the urinary trypsin inhibitors are discussed.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 9","pages":"1123-30"},"PeriodicalIF":0.0,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1123","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17558472","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: 21

Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of the inhibitor of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes). 蛇毒磷脂酶及其抑制剂序列同源性研究。保加利亚蝰蛇(Vipera ammodytes ammodytes, Serpentes)毒液中毒毒素抑制剂的初级结构。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-08-01 DOI: 10.1515/bchm2.1984.365.2.885

I Mancheva, T Kleinschmidt, B Aleksiev, G Braunitzer

{"title":"Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of the inhibitor of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).","authors":"I Mancheva, T Kleinschmidt, B Aleksiev, G Braunitzer","doi":"10.1515/bchm2.1984.365.2.885","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.885","url":null,"abstract":"We are presenting the first primary structure of a snake venom inhibitor. It was isolated from the neurotoxin vipoxin of the Bulgarian Viper (Vipera ammodytes ammodytes, Serpentes) which represents a complex of a strong toxic basic protein with phospholipase A2 activity (2 isoenzymes) and the nontoxic acidic component functioning as its inhibitor. The sequence was established by automatic degradation in a liquid phase sequenator on the S-carboxymethylated chain and on the peptides obtained by tryptic hydrolysis of the oxidized chain. A limited tryptic digestion of the oxidized chain provided the necessary overlapping peptides. The inhibitor consists of 122 amino-acid residues including 14 cysteine and 10 tyrosine residues and is thus similar to the phospholipases from snake venoms. A comparison of the inhibitor sequence with the primary structure of the phospholipase A2 (CM-II) from the Horned Adder (Bitis nasicornis) venom shows a surprising homology of 52%. The identical amino acids include the cysteine and tyrosine residues and are generally accumulated in the surroundings of cysteine residues. The histidine (pos. 47) in the active center of the phospholipase A2 is substituted by glutamine in the inhibitor, but the tryptophan (pos. 30) which is essential for the enzymatic activity is present. The significant homology between enzyme and inhibitor in the vipoxin complex is believed to originate from a gene duplication. The relatively late development of the reptiles and the snake venom complex explains the highly preserved structure compared to other enzyme-inhibitor systems.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 8","pages":"885-94"},"PeriodicalIF":0.0,"publicationDate":"1984-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.885","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17547209","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: 53

Tilorone acts as a lysosomotropic agent in fibroblasts. 蒂洛龙在成纤维细胞中作为溶酶体促增生剂。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-08-01 DOI: 10.1515/bchm2.1984.365.2.859

D K Gupta, V Gieselmann, A Hasilik, K von Figura

引用次数: 34

Intramolecular hydride transfer of a combined coenzyme-substrate analog by D- and L-lactate dehydrogenases. D-乳酸脱氢酶和l -乳酸脱氢酶联合辅酶-底物类似物的分子内氢化物转移。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-08-01 DOI: 10.1515/bchm2.1984.365.2.877

R Philipp, G L Long, W E Trommer

引用次数: 2

On the synthesis of a 32P-labelled Edman reagent for the sensitive identification of amino-acid derivatives. 合成一种32p标记的Edman试剂，用于氨基酸衍生物的灵敏鉴定。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-08-01 DOI: 10.1515/bchm2.1984.365.2.839

B E Ender, H G Gassen, W Machleidt

引用次数: 4

Phenylalkylsulfonyl derivatives as covalent inhibitors of penicillin amidase. 苯烷基磺酰衍生物作为青霉素酰胺酶的共价抑制剂。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-08-01 DOI: 10.1515/bchm2.1984.365.2.829

M Siewiński, M Kuropatwa, A Szewczuk

引用次数: 17