Shizuya Kabuto , Tomohisa Ogawa , Koji Muramoto , Vaughan Oosthuizen , Ryno J. Naude
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引用次数: 0
Abstract
The amino-acid sequence of α-amylase isolated from the pancreas of the ostrich, Struthio camelus was determined. The α-amylase (OPA) consisted of 497 amino acid residues with pyroglutamic acid at the N-terminus and no oligosaccharide. Amino acid identity between OPA and chicken, porcine and human pancreatic α-amylases individually, was found to be 88, 82 and 86%, respectively.
期刊介绍：
Comparative Biochemistry & Physiology (CBP) publishes papers in comparative, environmental and evolutionary physiology.
Part B: Biochemical and Molecular Biology (CBPB), focuses on biochemical physiology, primarily bioenergetics/energy metabolism, cell biology, cellular stress responses, enzymology, intermediary metabolism, macromolecular structure and function, gene regulation, evolutionary genetics. Most studies focus on biochemical or molecular analyses that have clear ramifications for physiological processes.
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