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Conformational studies on modified proteins and peptides. 3. Conformation of peptides obtained by cleavage of myoglobin at arginine peptide bonds.

作者信息

Atassi M Z, Singhal R P

出版信息

J Biol Chem. 1970 Oct 10;245(19):5122-8.

PMID:5528241
Abstract
摘要

相似文献

1
Conformational studies on modified proteins and peptides. 3. Conformation of peptides obtained by cleavage of myoglobin at arginine peptide bonds.修饰蛋白质和肽的构象研究。3. 通过肌红蛋白在精氨酸肽键处裂解得到的肽的构象
J Biol Chem. 1970 Oct 10;245(19):5122-8.
2
Conformational studies on modified proteins and peptides. Conformation of peptides with intact and overlapping helices obtained by cleavage of myoglobin at proline peptide bonds.修饰蛋白质和肽的构象研究。通过肌红蛋白在脯氨酸肽键处裂解获得的具有完整和重叠螺旋的肽的构象。
Biochemistry. 1970 Oct 27;9(22):4252-9. doi: 10.1021/bi00824a003.
3
Immunochemistry of sperm whale of myoglobin. IX. Specific interaction of peptides obtained by cleavage at arginine peptide bonds.抹香鲸肌红蛋白的免疫化学。IX. 通过精氨酸肽键裂解获得的肽段的特异性相互作用。
Biochemistry. 1971 May 11;10(10):1756-62. doi: 10.1021/bi00786a004.
4
Conformational studies on modified proteins and peptides. V. Conformation of myoglobin derivatives modified at two carboxyl groups.修饰蛋白质和肽的构象研究。V. 在两个羧基处修饰的肌红蛋白衍生物的构象
J Biol Chem. 1972 Sep 25;247(18):5980-6.
5
Immunochemistry of sperm-whale myoglobin. Conformation and immunochemistry of derivative reduced at some carboxyl groups by diborane.抹香鲸肌红蛋白的免疫化学。经乙硼烷在某些羧基处还原的衍生物的构象与免疫化学。
Biochemistry. 1972 Oct 10;11(21):3984-90. doi: 10.1021/bi00771a023.
6
Immunochemistry of sperm-whale myoglobin. XVII. Conformation and immunochemistry of derivatives modified at lysines 98, 140 and 145 by reaction with 3,3-tetramethyleneglutaric anhydride.抹香鲸肌红蛋白的免疫化学。十七。通过与3,3 - 四亚甲基戊二酸酐反应在赖氨酸98、140和145处修饰的衍生物的构象和免疫化学。
Biochim Biophys Acta. 1973 Dec 6;328(2):278-88.
7
Immunochemistry of sperm whale myoglobin. XV. Accurate delineation of the single antigenic reactive region in sequence 1-55 of myoglobin by chemical derivatives of the peptide carrying the region: conclusions relating to antigenic structures of proteins.抹香鲸肌红蛋白的免疫化学。十五。通过携带该区域的肽的化学衍生物精确描绘肌红蛋白序列1 - 55中的单一抗原反应区域:关于蛋白质抗原结构的结论
Immunochemistry. 1974 Feb;11(2):63-70. doi: 10.1016/0019-2791(74)90317-6.
8
Circular dichroism and optical rotatory dispersion of proteins and polypeptides.蛋白质和多肽的圆二色性与旋光色散
Methods Enzymol. 1973;27:675-735. doi: 10.1016/s0076-6879(73)27030-1.
9
The carboxymethylation of human metmyoglobin.人高铁肌红蛋白的羧甲基化作用
J Biol Chem. 1969 Apr 25;244(8):2195-203.
10
Optical rotatory dispersion and circular dichroism studies on insulin and its trypsin-modified derivatives.胰岛素及其胰蛋白酶修饰衍生物的旋光色散和圆二色性研究。
Arch Biochem Biophys. 1970 Sep;140(1):286-94. doi: 10.1016/0003-9861(70)90033-0.

引用本文的文献

1
Quantitative screening of clinical isolates for immunoglobulin A protease production.
J Clin Microbiol. 1983 Aug;18(2):365-71. doi: 10.1128/jcm.18.2.365-371.1983.
2
The formation and stabilization of protein structure.蛋白质结构的形成与稳定
Biochem J. 1972 Jul;128(4):737-49. doi: 10.1042/bj1280737.
3
-Galactosidase: immunological activity of ribosome-bound, growing polypeptide chains.β-半乳糖苷酶:核糖体结合的正在生长的多肽链的免疫活性。
Proc Natl Acad Sci U S A. 1972 Feb;69(2):412-6. doi: 10.1073/pnas.69.2.412.
4
Non-specific peptide size effects in the recognition by site-specific T-cell clones. Demonstration with a T site of myoglobin.位点特异性T细胞克隆识别中的非特异性肽大小效应。以肌红蛋白的一个T位点为例进行说明。
Biochem J. 1987 Sep 1;246(2):307-12. doi: 10.1042/bj2460307.
5
The limited proteolysis of tumor necrosis factor-alpha.
J Protein Chem. 1989 Oct;8(5):669-77. doi: 10.1007/BF01025607.
6
Site recognition by protein-primed T cells shows a non-specific peptide size requirement beyond the essential residues of the site. Demonstration by defining an immunodominant T site in myoglobin.蛋白质引发的T细胞对位点的识别显示,除了位点的必需残基外,还存在非特异性的肽大小要求。通过定义肌红蛋白中的免疫显性T细胞位点进行证明。
Biochem J. 1986 Nov 15;240(1):139-46. doi: 10.1042/bj2400139.
7
Restriction in the conformational flexibility of apoproteins in the presence of organic cosolvents: a consequence of the formation of "native-like conformation".在有机共溶剂存在下载脂蛋白构象灵活性的限制:“类天然构象”形成的结果。
J Protein Chem. 1992 Oct;11(5):527-38. doi: 10.1007/BF01025030.