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Immunochemistry of sperm whale myoglobin. VI. Preparation and conformational analysis of eight mammalian myoglobins.

作者信息

Atassi M Z

出版信息

Biochim Biophys Acta. 1970 Dec 22;221(3):612-22. doi: 10.1016/0005-2795(70)90233-3.

DOI:10.1016/0005-2795(70)90233-3
PMID:5499445
Abstract
摘要

相似文献

1
Immunochemistry of sperm whale myoglobin. VI. Preparation and conformational analysis of eight mammalian myoglobins.抹香鲸肌红蛋白的免疫化学。VI. 八种哺乳动物肌红蛋白的制备及构象分析。
Biochim Biophys Acta. 1970 Dec 22;221(3):612-22. doi: 10.1016/0005-2795(70)90233-3.
2
Immunochemistry of sperm whale myoglobin. VII. Correlation of immunochemical cross-reaction of eight myoglobins with structural similarity and its dependence on conformation.抹香鲸肌红蛋白的免疫化学。VII. 八种肌红蛋白免疫化学交叉反应与结构相似性的相关性及其对构象的依赖性。
Biochim Biophys Acta. 1970 Dec 22;221(3):623-35. doi: 10.1016/0005-2795(70)90234-5.
3
Immunochemistry of sperm-whale myoglobins prepared with various modified porphyrins and metalloporphyrins.用各种改性卟啉和金属卟啉制备的抹香鲸肌红蛋白的免疫化学。
Biochem J. 1967 Apr;103(1):29-35. doi: 10.1042/bj1030029.
4
Immunochemistry of sperm whale myoglobin. XIV. Role of histidines 12 and 24 in the antigenic structure.抹香鲸肌红蛋白的免疫化学。十四。组氨酸12和24在抗原结构中的作用。
Immunochemistry. 1973 Sep;10(9):601-6. doi: 10.1016/0019-2791(73)90161-4.
5
Immunochemistry of sperm whale myoglobin. II. Modification of the two tryptophan residues and their role in the conformation and antigen-antibody reaction.抹香鲸肌红蛋白的免疫化学。II. 两个色氨酸残基的修饰及其在构象和抗原-抗体反应中的作用。
Biochemistry. 1968 Feb;7(2):699-705. doi: 10.1021/bi00842a027.
6
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.
7
Immunochemistry of sperm whale myoglobin. IV. The role of the arginine residues in the conformation and differentiation of their roles in the antigenic reactivity.抹香鲸肌红蛋白的免疫化学。IV. 精氨酸残基在其构象及抗原反应性中不同作用的分化里的作用。
Biochemistry. 1969 Aug;8(8):3385-94. doi: 10.1021/bi00836a037.
8
Comparison of myoglobins from harbor seal, porpoise, and sperm whale. IV. Isolation and characterization of the tryptic peptides of porpoise myoglobin.斑海豹、鼠海豚和抹香鲸肌红蛋白的比较。IV. 鼠海豚肌红蛋白胰蛋白酶肽段的分离与鉴定
J Biol Chem. 1969 Apr 25;244(8):2159-66.
9
Studies on myoglobin from the finback whale (Balaenoptera physalus). Preparation, physicochemical and immunochemical characterization, differentiation from sperm-whale myoglobin, amino acid composition and end-terminal analyses.长须鲸肌红蛋白的研究。制备、理化及免疫化学特性、与抹香鲸肌红蛋白的鉴别、氨基酸组成及末端分析。
Biochem J. 1966 Jan;98(1):82-93. doi: 10.1042/bj0980082.
10
THE BINDING OF CUPRIC AND ZINC IONS TO CRYSTALLINE SPERM WHALE MYOGLOBIN.铜离子和锌离子与结晶态抹香鲸肌红蛋白的结合
J Mol Biol. 1965 May;12:130-7. doi: 10.1016/s0022-2836(65)80287-x.

引用本文的文献

1
Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region.血红蛋白中预选抗原区域之外的氨基酸替换会影响其与通过用合成区域免疫获得的单克隆抗体的结合。
J Protein Chem. 1993 Aug;12(4):403-12. doi: 10.1007/BF01025040.
2
The antibody response to myoglobin is independent of the immunized species. Analysis in terms of replacements in the antigenic sites and in environmental residues of the cross-reactions of fifteen myoglobins with sperm-whale myoglobin antisera raised in different species.对肌红蛋白的抗体反应与免疫物种无关。分析了在不同物种中产生的十五种肌红蛋白与抹香鲸肌红蛋白抗血清交叉反应的抗原位点和环境残基中的替换情况。
Biochem J. 1980 Dec 1;191(3):681-97. doi: 10.1042/bj1910681.
3
Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability.肌红蛋白抗原位点的最近邻分析。其取代可改变结合位点残基环境从而改变其特性和结合能力的最近邻残基。
Biochem J. 1980 Dec 1;191(3):673-80. doi: 10.1042/bj1910673.
4
Precise determination of protein antigenic structures has unravelled the molecular immune recognition of proteins and provided a prototype for synthetic mimicking of other protein binding sites.蛋白质抗原结构的精确测定揭示了蛋白质的分子免疫识别，并为其他蛋白质结合位点的合成模拟提供了原型。
Mol Cell Biochem. 1980 Aug 29;32(1):21-43. doi: 10.1007/BF00421293.
5
Distance calculation of residues neighbouring to lysozyme antigenic sites. Site-neighbouring residues whose evolutionary substitution can modify the characteristics and binding energy of the sites.溶菌酶抗原位点邻近残基的距离计算。其进化替代可改变抗原位点特征和结合能的位点邻近残基。
Biochem J. 1980 Apr 1;187(1):163-72. doi: 10.1042/bj1870163.
6
T-cell recognition and antigen presentation of myoglobin. Protein recognition by site-specific T-cell clones is influenced by amino acid substitutions outside the site.肌红蛋白的T细胞识别与抗原呈递。位点特异性T细胞克隆对蛋白质的识别受该位点以外氨基酸取代的影响。
Biochem J. 1989 Mar 15;258(3):645-51. doi: 10.1042/bj2580645.
7
Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 113-120 (antigenic site 4) of myoglobin.抗原位点外氨基酸替换对通过肽免疫获得的具有预定特异性的单克隆抗体与蛋白质结合的影响：以肌红蛋白的113 - 120区域（抗原位点4）为例
J Protein Chem. 1992 Dec;11(6):677-86. doi: 10.1007/BF01024969.
8
Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 56-62 (antigenic site 2) of myoglobin.抗原位点外氨基酸取代对通过肽免疫获得的具有预定特异性的单克隆抗体与蛋白质结合的影响：以肌红蛋白的56-62区域（抗原位点2）为例进行说明
J Protein Chem. 1992 Oct;11(5):455-65. doi: 10.1007/BF01025022.
9
Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 15-22 (antigenic site 1) of myoglobin.抗原位点外氨基酸取代对通过肽免疫获得的具有预定特异性的单克隆抗体结合蛋白质的影响：以肌红蛋白的15-22区域（抗原位点1）为例进行说明
J Protein Chem. 1992 Oct;11(5):445-54. doi: 10.1007/BF01025021.
10
Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 94-100 (antigenic site 3) of myoglobin.抗原位点外氨基酸取代对通过肽免疫获得的具有预定特异性的单克隆抗体结合蛋白质的影响：以肌红蛋白的94-100区域（抗原位点3）为例进行说明
J Protein Chem. 1992 Oct;11(5):433-44. doi: 10.1007/BF01025020.