Structural studies on calf lens γ-crystallin fraction IV: A comparison of the cysteine-containing tryptic peptides with the corresponding amino acid sequence of γ-crystallin fraction II

The primary structures of calf lens low molecular weight proteins, the γ-crystallins, are being studied. This report presents amino acid sequences of the cysteine containing peptides of γ-crystallin fraction IV which are compared with the primary structure of γ-crystallin fraction II. It is conclude...

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Bibliographic Details
Published inExperimental eye research Vol. 26; no. 3; pp. 291 - 304
Main Authors Slingsby, Christine, Croft, Laurie R.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.03.1978
Subjects
Amino Acid Sequence
Amino Acids - analysis
Animals
Cattle
Chemical Fractionation
Chemical Phenomena
Chemistry
Crystallins - analysis
Cysteine - analysis
cysteine residues
lens proteins
Peptides - analysis
protein stability
Thermolysin
γ-crystallins
lens proteins
γ-crystallins
cysteine residues
amino acid sequence
protein stability
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Summary:The primary structures of calf lens low molecular weight proteins, the γ-crystallins, are being studied. This report presents amino acid sequences of the cysteine containing peptides of γ-crystallin fraction IV which are compared with the primary structure of γ-crystallin fraction II. It is concluded that there are at least two similar proteins in fraction IV coded for by non-allelic structural genes.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-4835
1096-0007
DOI:10.1016/0014-4835(78)90076-3