Cloning and sequencing of a carp βs-crystallin cDNA

Tschining Chang, Wen Chang Chang

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The mRNAs were extracted from common carp (Cyprinus carpio) lenses, purified, reverse transcribed, dC tailed and cloned into Escherichia coli with pBR322 as vector. The cloning efficiency was around 1·107 colonies per μg of mRNA. A clone (pC20) was found by hybrid-arrested translation to contain the cDNA related to carp crystallins. However, comparison of the derived amino-acid sequence with bovine γ-II and βs-crystallins indicates that this carp crystallin sequence resembles closely the bovine βs-crystallin and should be better classified as such except that this fish sequence does not contain the N-terminal 'arm' of four amino-acid residues present in bovine βs-crystallin.

Original languageEnglish
Pages (from-to)89-92
Number of pages4
JournalBBA - Gene Structure and Expression
Volume910
Issue number1
DOIs
Publication statusPublished - Oct 9 1987
Externally publishedYes

Fingerprint

Crystallins
Carps
Cloning
Organism Cloning
Complementary DNA
Amino Acids
Messenger RNA
Fish
Escherichia coli
Lenses
Amino Acid Sequence
Fishes
Clone Cells

Keywords

  • (Carp lens)
  • cDNA cloning
  • Nucleotide sequence
  • β-Crystallin

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Cite this

Cloning and sequencing of a carp βs-crystallin cDNA. / Chang, Tschining; Chang, Wen Chang.

In: BBA - Gene Structure and Expression, Vol. 910, No. 1, 09.10.1987, p. 89-92.

Research output: Contribution to journalArticle

@article{156a717b279949949c263028298d291d,
title = "Cloning and sequencing of a carp βs-crystallin cDNA",
abstract = "The mRNAs were extracted from common carp (Cyprinus carpio) lenses, purified, reverse transcribed, dC tailed and cloned into Escherichia coli with pBR322 as vector. The cloning efficiency was around 1·107 colonies per μg of mRNA. A clone (pC20) was found by hybrid-arrested translation to contain the cDNA related to carp crystallins. However, comparison of the derived amino-acid sequence with bovine γ-II and βs-crystallins indicates that this carp crystallin sequence resembles closely the bovine βs-crystallin and should be better classified as such except that this fish sequence does not contain the N-terminal 'arm' of four amino-acid residues present in bovine βs-crystallin.",
keywords = "(Carp lens), cDNA cloning, Nucleotide sequence, β-Crystallin",
author = "Tschining Chang and Chang, {Wen Chang}",
year = "1987",
month = "10",
day = "9",
doi = "10.1016/0167-4781(87)90098-4",
language = "English",
volume = "910",
pages = "89--92",
journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",
issn = "0167-4781",
publisher = "Elsevier BV",
number = "1",

}

TY - JOUR

T1 - Cloning and sequencing of a carp βs-crystallin cDNA

AU - Chang, Tschining

AU - Chang, Wen Chang

PY - 1987/10/9

Y1 - 1987/10/9

N2 - The mRNAs were extracted from common carp (Cyprinus carpio) lenses, purified, reverse transcribed, dC tailed and cloned into Escherichia coli with pBR322 as vector. The cloning efficiency was around 1·107 colonies per μg of mRNA. A clone (pC20) was found by hybrid-arrested translation to contain the cDNA related to carp crystallins. However, comparison of the derived amino-acid sequence with bovine γ-II and βs-crystallins indicates that this carp crystallin sequence resembles closely the bovine βs-crystallin and should be better classified as such except that this fish sequence does not contain the N-terminal 'arm' of four amino-acid residues present in bovine βs-crystallin.

AB - The mRNAs were extracted from common carp (Cyprinus carpio) lenses, purified, reverse transcribed, dC tailed and cloned into Escherichia coli with pBR322 as vector. The cloning efficiency was around 1·107 colonies per μg of mRNA. A clone (pC20) was found by hybrid-arrested translation to contain the cDNA related to carp crystallins. However, comparison of the derived amino-acid sequence with bovine γ-II and βs-crystallins indicates that this carp crystallin sequence resembles closely the bovine βs-crystallin and should be better classified as such except that this fish sequence does not contain the N-terminal 'arm' of four amino-acid residues present in bovine βs-crystallin.

KW - (Carp lens)

KW - cDNA cloning

KW - Nucleotide sequence

KW - β-Crystallin

UR - http://www.scopus.com/inward/record.url?scp=0023649201&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023649201&partnerID=8YFLogxK

U2 - 10.1016/0167-4781(87)90098-4

DO - 10.1016/0167-4781(87)90098-4

M3 - Article

VL - 910

SP - 89

EP - 92

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

SN - 0167-4781

IS - 1

ER -