The substrate binding site of pepsin.
作者信息
Humphreys R E, Fruton J S
出版信息
Proc Natl Acad Sci U S A. 1968 Feb;59(2):519-25. doi: 10.1073/pnas.59.2.519.
Abstract
摘要
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The substrate binding site of pepsin.胃蛋白酶的底物结合位点。
Proc Natl Acad Sci U S A. 1968 Feb;59(2):519-25. doi: 10.1073/pnas.59.2.519.
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The amino acid sequence of Pseudomonas fluorescens azurin.荧光假单胞菌天青蛋白的氨基酸序列。
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引用本文的文献
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Fluorescence studies on the active sites of proteinases.蛋白酶活性位点的荧光研究。
Mol Cell Biochem. 1980 Sep 15;32(2):105-14. doi: 10.1007/BF00227803.
2
Studies on the extended active sites of acid proteinases.酸性蛋白酶扩展活性位点的研究。
Proc Natl Acad Sci U S A. 1974 Apr;71(4):1070-2. doi: 10.1073/pnas.71.4.1070.
3
Hydrolysis and transpeptidation of peptide substrates by acetyl-pepsin.乙酰胃蛋白酶对肽底物的水解和转肽作用。
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本文引用的文献
1
Specific inactivation of pepsin by a diazo ketone.重氮酮对胃蛋白酶的特异性失活作用。
Proc Natl Acad Sci U S A. 1966 Dec;56(6):1817-22. doi: 10.1073/pnas.56.6.1817.
2
SPECIFICITY OF PEPSIN AND ITS DEPENDENCE ON A POSSIBLE 'HYDROPHOBICBINDING SITE'.胃蛋白酶的特异性及其对可能的“疏水结合位点”的依赖性。
Nature. 1963 Sep 14;199:1094-5. doi: 10.1038/1991094a0.
3
Measurement of protein-binding phenomena by gel filtration.通过凝胶过滤法测定蛋白质结合现象。
Biochim Biophys Acta. 1962 Oct 8;63:530-2. doi: 10.1016/0006-3002(62)90124-5.
4
Peptide-protein interaction as studied by gel filtration.通过凝胶过滤研究的肽-蛋白质相互作用。
Biochemistry. 1966 Feb;5(2):673-83. doi: 10.1021/bi00866a038.
5
Pepsin as an esterase.胃蛋白酶作为一种酯酶。
J Am Chem Soc. 1967 Jan 4;89(1):187-8. doi: 10.1021/ja00977a062.
6
Studies on the specificity of pepsin.胃蛋白酶特异性的研究。
Biochemistry. 1967 Jun;6(6):1765-77. doi: 10.1021/bi00858a027.
7
New synthetic substrates for pepsin.
Biochemistry. 1966 Jul;5(7):2473-83. doi: 10.1021/bi00871a044.
8
Pepsin from pepsinogen. Preparation and properties.胃蛋白酶原转化为胃蛋白酶。制备方法及性质。
J Biol Chem. 1966 Nov 10;241(21):4940-50.
9
Inactivation of pepsin by diphenyldiazomethane.二苯基重氮甲烷对胃蛋白酶的灭活作用。
Proc Natl Acad Sci U S A. 1965 Oct;54(4):1161-7. doi: 10.1073/pnas.54.4.1161.
10
Acetylation of pepsin and pepsinogen.胃蛋白酶和胃蛋白酶原的乙酰化作用。
J Biol Chem. 1966 Jan 10;241(1):153-7.
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