The myofibrillar proteins, myosin and actin, were quantitated using N$ sp tau$-methylhistidine determined from selected avian white and red skeletal muscles of randomly chosen young and adult white Leghorn chickens. No significant difference (P = 0.01) was noted with respect to muscle type or age in N$ sp tau$-methylhistidine levels which ranged from 0.383 to 0.637 g/kg protein, translating into a myofibrillar protein content ranging between 532.68 to 579.77 g/kg protein. The connective tissue and collagen content, on the other hand, were calculated using 5-hydroxylysine levels in muscle tissue (0.276 to 1.273 g/kg protein) and were found to be significantly higher (P $<$ 0.01) in avian red muscle tissue ranging from 50.19 to 53.80 g/kg protein as compared to white muscle tissue (13.41 to 19.43 g/kg). / It has also been demonstrated that native skeletal muscle actin isolated from three different species, and cardiac muscle actin isolated from bovine and porcine muscle tissue, who highly conserved amino acid compositions and contain 1 mole of N$ sp tau$-methylhistidine per mole of actin.
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.61271 |
Date | January 1987 |
Creators | Khalili, Ali Djawad |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Master of Science (Department of Food Science and Agricultural Chemistry.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 000660299, proquestno: AAIMM75892, Theses scanned by UMI/ProQuest. |
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