α-晶状体蛋白的结构研究。
Structural studies of alpha-crystallin.
作者信息
Waley S G
出版信息
Biochem J. 1965 Sep;96(3):722-8. doi: 10.1042/bj0960722.
Abstract
- alpha-Crystallin has been isolated from the cortex of ox lens by isoelectric precipitation followed by chromatography on DEAE-cellulose. The amino acid composition is in agreement with that reported for alpha-crystallin prepared by a different method. There is one thiol group/20000g. of protein (20000 is the order of magnitude of the sub-unit molecular weight), and disulphide bonds are absent. 2. The thiol group has been alkylated with radioactive iodoacetate in the presence of urea. 3. Partial acid hydrolysis of the alkylated protein gives, according to the conditions, mainly three radioactive peptides or nearly exclusively one radioactive dipeptide. The dipeptide is N-seryl-(S-carboxymethyl)cysteine, Ser-CMCys. The two other peptides are probably the tripeptides related to Ser-CMCys. 4. The simplest interpretation of these results is that the sequence around the cysteine residue is a common structural feature of the sub-units of alpha-crystallin.
摘要
- 通过等电沉淀法，随后在二乙氨基乙基纤维素上进行色谱分离，从牛晶状体皮质中分离出α-晶状体蛋白。其氨基酸组成与通过不同方法制备的α-晶状体蛋白所报道的一致。每20000克蛋白质中有一个巯基（20000是亚基分子量的数量级），且不存在二硫键。2. 在尿素存在下，巯基已用放射性碘乙酸烷基化。3. 根据条件，对烷基化蛋白质进行部分酸水解主要产生三种放射性肽，或几乎仅产生一种放射性二肽。该二肽是N-丝氨酰-（S-羧甲基）半胱氨酸，即丝氨酸-羧甲基半胱氨酸（Ser-CMCys）。另外两种肽可能是与丝氨酸-羧甲基半胱氨酸相关的三肽。4. 对这些结果最简单的解释是，半胱氨酸残基周围的序列是α-晶状体蛋白亚基的共同结构特征。
相似文献
1
Structural studies of alpha-crystallin.α-晶状体蛋白的结构研究。
Biochem J. 1965 Sep;96(3):722-8. doi: 10.1042/bj0960722.
2
Structural studies on lens proteins.晶状体蛋白的结构研究。
Biochem J. 1967 Jul;104(1):128-34. doi: 10.1042/bj1040128.
3
Amino acid sequences around the cysteine residue of calf lens -crystallin.小牛晶状体β-晶状体蛋白半胱氨酸残基周围的氨基酸序列。
Biochem J. 1971 Aug;124(1):61-7. doi: 10.1042/bj1240061.
4
Further studies on the sub-units of alpha-crystallin.关于α-晶状体蛋白亚基的进一步研究。
Biochem J. 1966 Apr;99(1):179-88. doi: 10.1042/bj0990179.
5
STUDIES ON THE SUBUNITS OF ALPHA-CRYSTALLIN AND THEIR RECOMBINATION.α-晶状体蛋白亚基及其重组的研究
Exp Eye Res. 1964 Sep;3:239-47. doi: 10.1016/s0014-4835(64)80016-6.
6
PHYSICOCHEMICAL PROPERTIES OF ALPHA-CRYSTALLIN FROM CALF LENS COMPARED TO THOSE FROM OX LENS.与牛眼晶状体α-晶体蛋白相比，小牛眼晶状体α-晶体蛋白的物理化学性质
Can J Biochem. 1965 Mar;43:331-40. doi: 10.1139/o65-042.
7
Effects of modification of the sulhydryl groups of calf lens low molecular weight alpha-crystallin.小牛晶状体低分子量α-晶体蛋白巯基修饰的作用
Exp Eye Res. 1978 Apr;26(4):419-27. doi: 10.1016/0014-4835(78)90129-x.
8
Physicochemical characterization of a crystallin from the squid lens and its comparison with vertebrate lens crystallins.鱿鱼晶状体一种晶状体蛋白的物理化学特性及其与脊椎动物晶状体晶状体蛋白的比较。
J Biochem. 1984 Jan;95(1):75-82. doi: 10.1093/oxfordjournals.jbchem.a134605.
9
-Crystallin. Fractionation of subunits and sequence studies on an isolated polypeptide.-晶状体蛋白。亚基的分级分离及对一种分离出的多肽的序列研究。
Biochem J. 1971 Sep;124(2):345-55. doi: 10.1042/bj1240345.
10
Isoelectric focusing of crystallins in microsections of calf and adult bovine lens. Identification of water-insoluble crystallins complexing under nondenaturing conditions: demonstration of chaperone activity of alpha-crystallin.小牛和成年牛晶状体切片中晶状体蛋白的等电聚焦。鉴定在非变性条件下复合的水不溶性晶状体蛋白：证明α-晶状体蛋白的伴侣活性。
Ophthalmic Res. 1996;28(6):365-74. doi: 10.1159/000267931.
引用本文的文献
1
Studies on the sub-units of triose phosphate isomerase.三磷酸甘油醛异构酶亚基的研究。
Biochem J. 1968 May;107(6):737-44. doi: 10.1042/bj1070737.
2
Possible reactions of 1,2-naphthaquinone in the eye.1,2-萘醌在眼部的可能反应。
Biochem J. 1967 Mar;102(3):853-63.
3
Structural studies on lens proteins.晶状体蛋白的结构研究。
Biochem J. 1967 Jul;104(1):128-34. doi: 10.1042/bj1040128.
4
Further studies on the sub-units of alpha-crystallin.关于α-晶状体蛋白亚基的进一步研究。
Biochem J. 1966 Apr;99(1):179-88. doi: 10.1042/bj0990179.
5
N-terminal sequences of alpha-crystallin.α-晶状体蛋白的N端序列
Biochem J. 1969 Dec;115(4):789-96. doi: 10.1042/bj1150789.
6
Amino acid sequences around the cysteine residue of calf lens -crystallin.小牛晶状体β-晶状体蛋白半胱氨酸残基周围的氨基酸序列。
Biochem J. 1971 Aug;124(1):61-7. doi: 10.1042/bj1240061.
7
Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase.兔肌肉磷酸丙糖异构酶半胱氨酸残基周围的氨基酸序列。
Biochem J. 1971 Apr;122(2):209-18. doi: 10.1042/bj1220209.
本文引用的文献
1
Biochemistry of bovine lens proteins. I. Isolation and characterization of adult alpha-crystallins.牛晶状体蛋白的生物化学。I. 成年α-晶状体蛋白的分离与特性分析。
Biochim Biophys Acta. 1962 Jul 2;60:205-16. doi: 10.1016/0006-3002(62)90396-7.
2
[Quantitative determination of amino acid composition of protein hydrolysates by combined electrophoresis and chromatography].[通过电泳和色谱联用法定量测定蛋白质水解产物的氨基酸组成]
Hoppe Seylers Z Physiol Chem. 1955;299(5-6):258-76.
3
New method for fractionation of lens proteins.晶状体蛋白分级分离的新方法。
AMA Arch Ophthalmol. 1954 Apr;53(4):481-6. doi: 10.1001/archopht.1955.00930010483004.
4
METHODS OF ISOLATION OF ALPHA, BETA, AND GAMMA CRYSTALLINS AND THEIR SUBGROUPS.α、β和γ晶状体蛋白及其亚组的分离方法。
Invest Ophthalmol. 1964 Apr;3:182-93.
5
Splitting and recombination of alpha-crystallin.α-晶状体蛋白的分裂与重组
Exp Eye Res. 1962 Jun;1:300-5. doi: 10.1016/s0014-4835(62)80015-3.
6
Isolation and properties of alpha-crystallin from the bovine lens.牛晶状体α-晶体蛋白的分离与特性
Arch Biochem Biophys. 1959 Oct;84:512-27. doi: 10.1016/0003-9861(59)90612-5.
7
An electrophoretic study of soluble lens proteins from different species.不同物种晶状体可溶性蛋白质的电泳研究。
Am J Ophthalmol. 1961 Feb;51:305-14.
8
An amino acid sequence in the active centre of phosphoglucomutase.磷酸葡萄糖变位酶活性中心的氨基酸序列。
Biochem J. 1961 Jun;79(3):456-69. doi: 10.1042/bj0790456.
9
Immunochemical analyses of lens protein separations.晶状体蛋白分离物的免疫化学分析。
Arch Biochem Biophys. 1961 Mar;92:512-24. doi: 10.1016/0003-9861(61)90392-7.
10
The amino acid sequence around the reactive serine residue of some proteolytic enzymes.一些蛋白水解酶的活性丝氨酸残基周围的氨基酸序列。
Biochem J. 1960 Oct;77(1):149-63. doi: 10.1042/bj0770149.
Zotero 插件