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牛视紫红质的氨基末端和羧基末端序列。

The amino- and carboxyl-terminal sequence of bovine rhodopsin.

作者信息

Hargrave P A, Fong S L

出版信息

J Supramol Struct. 1977;6(4):559-70. doi: 10.1002/jss.400060409.

DOI:10.1002/jss.400060409
PMID:592823
Abstract

The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment. The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala. Upon short-term digestion of rod outer segment (ROS) membranes with thermolysin, opsin (similar to 35,000 daltons) is converted to a membrane-bound fragment O' (similar to 30,500 daltons) and 2 peptides containing 12 amino acids are released from the carboxyl terminus of rhodopsin into the supernatant. Upon long-term digestion of ROS with thermolysin, opsin and O' are replaced by the membrane-bound fragments F1 (similar to 25,000 daltons), and F2 (similar 9,500 daltons). When 32P-ROS are digested, F2 carries the 32P. Both O' and F1 contain the amino-terminal glycopeptide.

摘要

牛视紫红质的氨基末端被封闭,其序列为x-甲硫氨酸-天冬酰胺(CHO)-甘氨酸-苏氨酸-谷氨酸-甘氨酸-脯氨酸-天冬酰胺-苯丙氨酸-酪氨酸-缬氨酸-脯氨酸-苯丙氨酸-丝氨酸-天冬酰胺(CHO)-赖氨酸-苏氨酸-甘氨酸-缬氨酸-缬氨酸-精氨酸,其中CHO代表碳水化合物连接位点。视紫红质的羧基末端序列为缬氨酸-丝氨酸-赖氨酸-苏氨酸-谷氨酸-苏氨酸-丝氨酸-谷氨酰胺-缬氨酸-丙氨酸-脯氨酸-丙氨酸。用嗜热菌蛋白酶对杆状外段(ROS)膜进行短期消化后,视蛋白(约35,000道尔顿)转化为膜结合片段O′(约30,500道尔顿),并且从视紫红质的羧基末端释放出2个含12个氨基酸的肽进入上清液。用嗜热菌蛋白酶对ROS进行长期消化后,视蛋白和O′被膜结合片段F1(约25,000道尔顿)和F2(约9,500道尔顿)取代。当用32P标记的ROS进行消化时,F2带有32P。O′和F1都含有氨基末端糖肽。

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引用本文的文献

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Annu Rev Physiol. 2003;65:851-79. doi: 10.1146/annurev.physiol.65.092101.142611. Epub 2002 May 1.
2
Rhodopsin phosphorylation occurs at metarhodopsin II level.视紫红质磷酸化发生在变视紫红质II水平。
Biophys Struct Mech. 1983;9(4):259-67. doi: 10.1007/BF00535661.
3
In vitro biosynthesis, core glycosylation, and membrane integration of opsin.视蛋白的体外生物合成、核心糖基化及膜整合
J Cell Biol. 1981 Jul;90(1):236-42. doi: 10.1083/jcb.90.1.236.
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Biophys Struct Mech. 1983;9(4):235-44. doi: 10.1007/BF00535659.
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Biochem J. 1985 Dec 15;232(3):669-72. doi: 10.1042/bj2320669.
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