Literature DB >> 6767558

[Purification and partial sequence of a hydrophobic polypeptide from BNPS-skatole cleaved bovine rhodopsin].

C Pellicone, P Bouillon, N Virmaux.   

Abstract

Rhodopsin isolated from outer segments of cattle retinas was cleaved at tryptophan residues by the BNPS-skatole. One of the polypeptides obtained S 5 (molecular weight about 12,000) of hydrophobic nature was isolated and the sequence of its 50 first residues revealed 60% of hydrophobic AA.

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Year:  1980        PMID： 6767558

Source DB:  PubMed          Journal:  C R Seances Acad Sci D        ISSN： 0567-655X


  5 in total

Review 1.  The opsin family of proteins.

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

2.  Sequence variability in the retinal-attachment domain of mammalian rhodopsins.

Authors:  D J Pappin; J B Findlay
Journal:  Biochem J       Date:  1984-02-01       Impact factor: 3.857

3.  The structure of bovine rhodopsin.

Authors:  P A Hargrave; J H McDowell; D R Curtis; J K Wang; E Juszczak; S L Fong; J K Rao; P Argos
Journal:  Biophys Struct Mech       Date:  1983

4.  Site of attachment of retinal in bacteriorhodopsin.

Authors:  H Bayley; K S Huang; R Radhakrishnan; A H Ross; Y Takagaki; H G Khorana
Journal:  Proc Natl Acad Sci U S A       Date:  1981-04       Impact factor: 11.205

5.  Structural studies on membrane-bound bovine rhodopsin.

Authors:  E Mullen; M Akhtar
Journal:  Biochem J       Date:  1983-04-01       Impact factor: 3.857
  5 in total

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