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dc.contributor.authorGoodson, John Arthur
dc.description.abstractMyoglobin has an important physiological role in vertebrates, and as the primary sarcoplasmic pigment in meat, influences quality perception and consumer acceptability. In this study, the amino acid sequences of Japanese quail and northern bobwhite myoglobin were deduced by cDNA cloning of the coding sequence from mRNA. Japanese quail myoglobin was isolated from quail cardiac muscles, purified using ammonium sulfate precipitation and gel-filtration, and subjected to multiple enzymatic digestions. Mass spectrometry corroborated the deduced protein amino acid sequence at the protein level. Sequence analysis revealed both species’ myoglobin structures consist of 153 amino acids, differing at only three positions. When compared with chicken myoglobin, Japanese quail showed 98% sequence identity, and northern bobwhite 97% sequence identity. The myoglobin in both quail species contained eight histidine residues instead of the nine present in chicken and turkey.
dc.subjectJapanese quail
dc.subjectnorthern bobwhite
dc.subjectcDNA cloning
dc.subjectprimary structure
dc.subjectCoturnix japonica
dc.subjectColinus virginianus
dc.titleAmino acid sequence of Japanese quail (Coturnix japonica) and northern bobwhite (Colinus virginianus) myoglobin
dc.description.departmentFood Science and Technology
dc.description.majorFood Science
dc.description.advisorAnand Mohan
dc.description.committeeAnand Mohan
dc.description.committeeRakesh Singh
dc.description.committeeRobert Beckstead

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