Biochimica et Biophysica Acta (BBA) - Protein Structure最新文献_第10页

Superoxide dismutase from the archaebacterium Thermoplasma acidophilum 嗜酸热原细菌的超氧化物歧化酶

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90046-5

Karen B. Searcy , Dennis G. Searcy

引用次数: 36

Determination of surface tensions of proteins II. Surface tension of serum albumin, altered at the protein-air interface 蛋白质表面张力的测定2。血清白蛋白的表面张力，在蛋白质-空气界面处改变

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90050-7

D.R. Absolom , C.J. Van Oss , W. Zingg , A.W. Neumann

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引用次数: 56

The amino acid sequence of the amino-terminal cyanogen bromide fragment of Tachypleus tridentatus hemocyanin α chain 三叉鱼血青素α链氨基末端溴化氰片段的氨基酸序列

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90051-9

Takayuki Nemoto, Takashi Takagi

引用次数: 5

Kinetics of the neutral transition of human serum albumin 人血清白蛋白中性转变的动力学

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90056-8

Jørgen Jacobsen, Thyge Faerch

引用次数: 15

The effects of limited proteolysis by trypsin on human haptoglobin 胰蛋白酶有限蛋白水解对人触珠蛋白的影响

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90043-X

Iwona Katnik, Wanda Dobryszycka

引用次数: 3

Determination of the surface tension of proteins I. Surface tension of native serum proteins in aqueous media 蛋白质表面张力的测定。天然血清蛋白在水介质中的表面张力

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90049-0

C.J. Van Oss , D.R. Absolom , A.W. Neumann , W. Zingg

{"title":"Determination of the surface tension of proteins I. Surface tension of native serum proteins in aqueous media","authors":"C.J. Van Oss , D.R. Absolom , A.W. Neumann , W. Zingg","doi":"10.1016/0005-2795(81)90049-0","DOIUrl":"10.1016/0005-2795(81)90049-0","url":null,"abstract":"<div><p>The desorption patterns of serum proteins in hydrophobic chromatography suggest that serum proteins that remain immersed in an aqueous medium and do not become involved in a protein-air interface are very hydrophilic. Contact angle measurements on fairly thick layers of hydrated serum proteins, formed on ultrafiltration membranes, yield surface tensions that correlate well with the degree of hydrophilicity derived from desorption data obtained by hydrophobic chromatography. For further confirmation the absorptivity of four human serum proteins was measured with respect to surfaces of different polymers of various surface tensions, from solution in aqueous solvents of different surface tensions. The surface tension of the solvent from which a dissolved protein adsorbs to precisely the same extent onto all solid substrates (regardless of their surface tensions) is equal to the surface tension of that protein. The surface tensions found by the contact angle (first value given) and by the protein adsorption methods (second value given) were, in erg/cm<sup>2</sup>; <em>α</em><sub>2</sub>-macroglobulin, 71.0, 71.0; serum albumin, 70.5, 70.2; immunoglobulin M, 69.5, 69.4; immunoglobulin G, 67.4, 67.7.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90049-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17233099","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: 72

Titles of related papers in other sections 其他章节相关论文的标题

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-08-28 DOI: 10.1016/0005-2795(81)90059-3

引用次数: 0

Antithrombin III does not have bound glucocerebroside 抗凝血酶III没有结合糖脑苷

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-07-28 DOI: 10.1016/0005-2795(81)90250-6

George L. Dale, Beryl Westwood

引用次数: 2

Application of photoactivatable fluorescent active-site directed probes to serine-containing enzymes 光活化荧光活性位点定向探针在含丝氨酸酶中的应用

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-07-28 DOI: 10.1016/0005-2795(81)90236-1

Kimon J. Angelides

{"title":"Application of photoactivatable fluorescent active-site directed probes to serine-containing enzymes","authors":"Kimon J. Angelides","doi":"10.1016/0005-2795(81)90236-1","DOIUrl":"10.1016/0005-2795(81)90236-1","url":null,"abstract":"<div><p>A photoactivatable fluorescent anthraniloyl group has been directed to the active-site serine group of α-chymotrypsin and trypsin. The acylated derivatives are nonfluorescent until irradiated. When activated by light a highly reactive nitrene is generated which is capable of covalent insertion into the protein matrix. The resultant insertion product of this photolysis is a highly fluorescent reporter group which has little rotational mobility and is cross-linked through the serine to the protein matrix in the active site region of the protein. Because of the sensitivity to the polarity of the environment shown by the anthraniloyl chromophore, the dipolar relaxation characteristics of the cross-linked enzyme and deacylated enzyme were determined. These measurements show that little relaxation occurs on the nanosecond time scale for the cross-linked enzyme, but upon deacylation of the serine increased dipolar relaxation of the protein with the attached reporter group is observed. The use of these active-site directed photoactivatable fluorescent probes can be extended to probe the active-site structure of complex enzymes and conformational dynamics of active-site regions in proteins and to serve as potential functional site labels in fluorescence resonance energy transfer measurements.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90236-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17845213","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: 6

Conformational properties of the protease from Staphylococcus aureus studied by circular dichroism 用圆二色性研究金黄色葡萄球菌蛋白酶的构象性质

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-07-28 DOI: 10.1016/0005-2795(81)90241-5

Bruno Jirgensons

引用次数: 2