Biochemical comparison of γ-crystallins from duck and frog eye lenses

Shyh Horng Chiou; Wen Chang Chang; Jane Kuo; Fu Ming Pan; Tung Bin Lo

doi:10.1016/0014-5793(86)80250-2

Biochemical comparison of γ-crystallins from duck and frog eye lenses

Shyh Horng Chiou, Wen Chang Chang, Jane Kuo, Fu Ming Pan, Tung Bin Lo

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

19 Citations (Scopus)

Abstract

A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystalline were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.

Original language	English
Pages (from-to)	219-222
Number of pages	4
Journal	FEBS Letters
Volume	196
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(86)80250-2
Publication status	Published - Feb 17 1986
Externally published	Yes

Keywords

Duck lens)Amino acid composition Peptide mapping Sequence homology
γ-Crystallin(Frog lens

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(86)80250-2

Cite this

@article{dca377112cce4d53b111a53e2f84575c,

title = "Biochemical comparison of γ-crystallins from duck and frog eye lenses",

abstract = "A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystalline were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.",

keywords = "Duck lens)Amino acid composition Peptide mapping Sequence homology, γ-Crystallin(Frog lens",

author = "Chiou, {Shyh Horng} and Chang, {Wen Chang} and Jane Kuo and Pan, {Fu Ming} and Lo, {Tung Bin}",

year = "1986",

month = feb,

day = "17",

doi = "10.1016/0014-5793(86)80250-2",

language = "English",

volume = "196",

pages = "219--222",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Biochemical comparison of γ-crystallins from duck and frog eye lenses

AU - Chiou, Shyh Horng

AU - Chang, Wen Chang

AU - Kuo, Jane

AU - Pan, Fu Ming

AU - Lo, Tung Bin

PY - 1986/2/17

Y1 - 1986/2/17

N2 - A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystalline were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.

AB - A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystalline were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.

KW - Duck lens)Amino acid composition Peptide mapping Sequence homology

KW - γ-Crystallin(Frog lens

UR - http://www.scopus.com/inward/record.url?scp=0023051606&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023051606&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(86)80250-2

DO - 10.1016/0014-5793(86)80250-2

M3 - Article

C2 - 3485058

AN - SCOPUS:0023051606

SN - 0014-5793

VL - 196

SP - 219

EP - 222

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Biochemical comparison of γ-crystallins from duck and frog eye lenses

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this