Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver

Pedro Gonzalez; P. Vasantha Rao; J. Samuel Zigler

doi:10.1006/bbrc.1993.1302

Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver

Pedro Gonzalez, P. Vasantha Rao, J. Samuel Zigler

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH:quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of ζ-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5′ and 796 of the 3′ non-translated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.

Original language	English (US)
Pages (from-to)	902-907
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	191
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1993.1302
State	Published - Mar 31 1993
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1006/bbrc.1993.1302

Cite this

@article{15255092a65e471aadff6a793f336bb3,

title = "Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver",

abstract = "Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH:quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of ζ-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5′ and 796 of the 3′ non-translated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.",

author = "Pedro Gonzalez and Rao, {P. Vasantha} and Zigler, {J. Samuel}",

year = "1993",

month = mar,

day = "31",

doi = "10.1006/bbrc.1993.1302",

language = "English (US)",

volume = "191",

pages = "902--907",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver

AU - Gonzalez, Pedro

AU - Rao, P. Vasantha

AU - Zigler, J. Samuel

PY - 1993/3/31

Y1 - 1993/3/31

N2 - Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH:quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of ζ-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5′ and 796 of the 3′ non-translated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.

AB - Zeta-crystallin is an enzyme-crystallin highly expressed in the lens of some hystricomorph rodents and camels. It has been shown to have a novel NADPH:quinone oxidoreductase activity and is present at enzymatic levels in a variety of tissues from various mammals. We report here the cDNA cloning of ζ-crystallin from a human liver library. One clone with the complete open reading frame was obtained. Ten nucleotides of the 5′ and 796 of the 3′ non-translated regions are present in the clone including two possible polyadenylation signals. The deduced amino acid sequence is 328 residues long with a calculated molecular mass of 34910 daltons and isoelectric point of 8.73. It shows 84% identity with the guinea pig protein.

UR - http://www.scopus.com/inward/record.url?scp=0027306028&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027306028&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1993.1302

DO - 10.1006/bbrc.1993.1302

M3 - Article

C2 - 8466529

AN - SCOPUS:0027306028

SN - 0006-291X

VL - 191

SP - 902

EP - 907

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Molecular cloning and sequencing of ζ-crystallin/quinone reductase cDNA from human liver

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this