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1.
Eur J Biochem ; 141(1): 131-40, 1984 May 15.
Article in English | MEDLINE | ID: mdl-6723655

ABSTRACT

The amino acid sequences of the alpha-crystallin A chains of 28 mammalian species, representing 14 different orders, have been analyzed, mainly on the basis of amino acid compositions of the composing peptides. The alpha A sequences of chicken and a frog have been completely determined by Edman degradation. A method is described to transport eye lenses, to be used for protein sequence studies, at ambient temperature in a solution of guanidine . HCl. The number of cysteine residues in different alpha A chains could be determined by alkaline urea gel electrophoresis after aminoethylation . In some cases the alpha A chains have been isolated from total lens extracts in a single ion-exchange chromatographic step. The average rate of substitutions in the evolution of the alpha A chains is moderately slow, approximately 3 amino acid substitutions per 100 residues in 100 million years, but varies considerably in different lineages. Substitutions involving changes in charge are strongly underrepresented; the alpha A chains tend to keep their net charge constant throughout evolution. Analysis of the types of substitutions suggests a directional trend leading to an increase in functional density of alpha A in the course of evolution.


Subject(s)
Crystallins , Amino Acid Sequence , Amino Acids/analysis , Animals , Anura , Biological Evolution , Chemical Phenomena , Chemistry , Chickens , Crystallins/genetics , Mammals , Peptide Fragments/analysis , Species Specificity
2.
Biochim Biophys Acta ; 491(2): 573-80, 1977 Apr 25.
Article in English | MEDLINE | ID: mdl-870070

ABSTRACT

As part of a study of the evolutionary development of the eye lens protein alpha-crystallin the 173-residue A chain of this protein has been studied in elephant, whale, hyrax and rhinoceros. The primary structures were inferred mainly from amino acid compositions of peptides obtained by enzymic digestions and CNBr cleavage. The positions of substitutions, as compared to the known bovine A chain, were confirmed by Edman degradation. In accordance with the previously observed slow rate of evolution of the A chain only a small number of substitutions was found among these species. Elephant and hyrax share a number of unique substitutions, strongly indicating a common ancestry of these two species within the mammalian class.


Subject(s)
Cetacea , Crystallins , Elephants , Hyraxes , Mammals , Perissodactyla , Whales , Amino Acid Sequence , Animals , Peptide Fragments/analysis , Species Specificity , Trypsin
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