Literature DB >> 1627174

Facile cloning and sequencing of S-crystallin genes from octopus lenses based on polymerase chain reaction.

C W Lin1, S H Chiou.   

Abstract

S-crystallin is a major lens protein present in the octopus and squid of Cephalopods. To facilitate the cloning of the protein, cDNA was constructed from the poly(A)+RNA of octopus lenses, and amplification by polymerase chain reaction (PCR) was carried out with two primers designed according to the 5'- and 3'-coding regions of S-crystallin gene. Sequencing two of 15 positive clones obtained shows 37-44% similarity in nucleotide and 23-30% similarity in amino acid sequences as compared with mammalian glutathione S-transferases (GST), revealing that S-crystallins exist as a multigene family and probably derived from GST by gene duplication and subsequent mutational base replacements.

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Year:  1992        PMID: 1627174

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  3 in total

1.  Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin.

Authors:  S S Tang; C C Lin; G G Chang
Journal:  J Protein Chem       Date:  1994-10

2.  Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity.

Authors:  C C Chuang; S H Wu; S H Chiou; G G Chang
Journal:  Biophys J       Date:  1999-02       Impact factor: 4.033

3.  Octopus S-crystallins with endogenous glutathione S-transferase (GST) activity: sequence comparison and evolutionary relationships with authentic GST enzymes.

Authors:  S H Chiou; C W Yu; C W Lin; F M Pan; S F Lu; H J Lee; G G Chang
Journal:  Biochem J       Date:  1995-08-01       Impact factor: 3.857

  3 in total

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