The Amino‐Acid Sequences of the α‐Crystallin A Chains of Red Kangaroo and Virginia Opossum
- 1 August 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 67 (2) , 503-510
- https://doi.org/10.1111/j.1432-1033.1976.tb10716.x
Abstract
The amino acid sequence of the A chain of the eye lens protein α‐srystallin from the red kangaroo (Macropus rufus) was completely determined by manual Edman degradation of tryptic, thermolytic and cyanogen bromide peptides. The sequence of the α‐crystallin A chain from the Virginia opossum (Didelphis marsupialis) was deduced from amino acid analyses and partial Edman degradation of peptides. The 173‐residue A chains of kangaroo and opossum differ in six positions, whereas comparison with the bovine α‐crystallin A chain reveals 17 and 22 substitutions, respectively. Most substitutions occur in the COOH‐terminal part of the chain.Keywords
This publication has 21 references indexed in Scilit:
- Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageingNature, 1975
- The amino acid sequence of the A chain of human α‐crystallinFEBS Letters, 1975
- Primary Structures of the alpha-Crystallin A Chains of Seven Mammalian SpeciesEuropean Journal of Biochemistry, 1975
- The Amino‐Acid Sequence of the αB2 Chain of Bovine α‐CrystallinEuropean Journal of Biochemistry, 1974
- Opossum Hb chain sequence and neutral mutation theoryNature, 1974
- Intracellular Carboxy‐Terminal Degradation of the αA Chain of α‐CrystallinEuropean Journal of Biochemistry, 1974
- The Amino‐Acid Sequence of the αA2 Chain of Bovine α‐CrystallinEuropean Journal of Biochemistry, 1973
- Fluorescamine: A Reagent for Assay of Amino Acids, Peptides, Proteins, and Primary Amines in the Picomole RangeScience, 1972
- An improved method for the recovery of compounds from paper chromatogramsJournal of Chromatography A, 1972
- Separation of dansyl-amino acids by polyamide layer chromatographyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967