The amino- and carboxyl-terminal sequence of bovine rhodopsin
✍ Scribed by Hargrave, Paul A. ;Fong, Shao-Ling
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 621 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
✦ Synopsis
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 (∼ 35,000 daltons) is converted to a membrane‐bound fragment O′ (∼ 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 F~1~ (∼25,000 daltons), and F~2~ (∼9,500 daltons). When ^32^P‐ROS are digested, F~2~ carries the ^32^P. Both O′ and F~1~ contain the amino‐terminal glycopeptide.
📜 SIMILAR VOLUMES
Proteins and peptides are digested with anhydrous hydrazine and the free amino acids, released from their carboxyl termini, are analyzed by reverse-phase chromatography as phenylthiocarbamyl (PTC) derivatives. Most of the potentially interfering hydrazides are removed due to the insolubility of thei