Purification and properties of the low-molecular-weight alpha-crystallin from normal goat lens: comparison with bovine lens.
Low-molecular-weight alpha-crystallin (alpha L-crystallin) isolated from decapsulated lens of goat (Capra hiscus) has been purified to an apparently homogeneous population. Goat alpha L-crystallin closely resembles its bovine counterpart in size, shape, exposition of sulfhydryl groups, subunit composition and the nature of its UV-absorption profile. Like bovine alpha L-crystallin, dissociated subunits of goat alpha L-crystallin assemble upon reassociation into a particle of almost half the size of the native one. However, subunits of goat alpha L-crystallin are found to contain more aromatic amino acid residues than those of bovine subunits leading to a higher value of extinction coefficient (E1cm1%) at 280 nm for the goat protein.
Roy
B
B
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Bidhannagar, Calcutta, India.
Ghosh
S K
SK
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003459:Crystallins / Q000737:chemistry* / Q000302:isolation & purification; D004228:Dithionitrobenzoic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D006041:Goats / Q000378:metabolism*; D007908:Lens, Crystalline / Q000737:chemistry*; D008623:Mercaptoethanol; D008854:Microscopy, Electron; D008970:Molecular Weight; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D003459:Crystallins; D008623:Mercaptoethanol; D004228:Dithionitrobenzoic Acid