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Literature DB >> 861254

The amino-terminal tryptic peptide of bovine rhodopsin. A glycopeptide containing two sites of oligosaccharide attachment.

Abstract

A glycopeptide (T1) composed of 16 amino acids has been isolated from a tryptic digest of bovine rhodopsin. Its sequence is Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys. Both rhodopsin and peptide T1 are blocked at their amino terminals. When a method specific for isolating amino-terminal tryptic peptides from proteins is applied to rhodopsin, peptide T1 is demonstrated to be the amino-terminal peptide of rhodopsin. Peptide T1 contains two sites at which carbohydrate is attached, whereas rhodopsin was previously thought to contain only a single such site.

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Year: 1977 PMID： 861254 DOI： 10.1016/0005-2795(77)90216-1

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

24 in total

Review 1. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).

Authors: D C Teller; T Okada; C A Behnke; K Palczewski; R E Stenkamp
Journal: Biochemistry Date: 2001-07-03 Impact factor: 3.162

Review 2. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors.

Authors: T M Savarese; C M Fraser
Journal: Biochem J Date: 1992-04-01 Impact factor: 3.857

3. Point mutations in bovine opsin can be classified in four groups with respect to their effect on the biosynthetic pathway of opsin.

Authors: G L DeCaluwé; W J DeGrip
Journal: Biochem J Date: 1996-12-15 Impact factor: 3.857

Review 4. The opsin family of proteins.

Authors: J B Findlay; D J Pappin
Journal: Biochem J Date: 1986-09-15 Impact factor: 3.857

5. Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin.

Authors: M Brett; J B Findlay
Journal: Biochem J Date: 1983-06-01 Impact factor: 3.857

The amino-terminal tryptic peptide of bovine rhodopsin. A glycopeptide containing two sites of oligosaccharide attachment.

Review 1. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).

Review 2. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors.

3. Point mutations in bovine opsin can be classified in four groups with respect to their effect on the biosynthetic pathway of opsin.

Review 4. The opsin family of proteins.

5. Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin.

6. Topography of the rhodopsin molecule. Identification of the domain phosphorylated.

7. Messenger RNA of opsin from bovine retina: isolation and partial sequence of the in vitro translation product.

8. A Drosophila metallophosphoesterase mediates deglycosylation of rhodopsin.

9. Development of visual cells in the Pacific bluefin tuna Thunnus orientalis.

10. Projection structure of frog rhodopsin in two crystal forms.