Identification of the meat of the different species of birds using the quantitative analysis of the descriptive shapes of the crystalline myosin [electronic resource].

By: Contributor(s): Language: English Summary language: Arabic Description: p.87-104Other title:
  • التعرف علي لحوم أنواع الطيور المختلفة باستخدام التحليل الكمي للأشكال الوصفية من بللورات الميوسين [Added title page title]
Uniform titles:
  • Mansoura Veterinary Medical Journal, 2009 v. 11 (2) [electronic resource].
Subject(s): Online resources: In: Mansoura Veterinary Medical Journal 2009.v.11(2)Summary: Myosin is the main contractile protein of the muscles. Crystalline myosin could be Prepared in the form of needle crystals. The different rearrangements of such needles together may forming different descriptive shapes which may be used for meat identification of bird species. Three fresh thigh muscles from each species of the five studied species of birds were homogenized for preparation of their crystalline myosins. The results indicated presence of nine different descriptive shapes in the studies species of birds, the (most) characteristic shapes and their percentages were recorded for each species as following : for Fattening broiler chickens : Large thick needle - like crystals (18.9%) and contacted myosin crystals (5.22%), for Native broiler chickens: Branched point - like crystals (5.93%), large thick needle - like crystals (14.23%)and Contacted myosin crystals (8.51%), for Pigeons : Long branched stem - like crystals (16.97%), Short branched stem- like crystals (21.86%), for Ibises : X - litter shape - like crystals, (5.01%) and Contacted myosin crystals (15.93% ), and for Ducks : Frond shape - like crystals (3.57%), K - litter shape - like crystals (6.85%), and Short branched stem - like crystals (20.06%). For more improvement of such method for further confirmation of species, it could be suggested that the myosin ( crystals, solutions, molecules and subfraqment -1-crystals) should be studied by different ways to understanding the species differences in their (total compositions and amino acids either contents or sequences ) in the presence of fixed in vivo and in vitro factors, Also, the negative staining with fixation of different crystalline myosins for electron microscopical study and the x- ray diffraction patterns analysis on myosin crystals and the crystals of myosin subfragment- 1 should be studied for further confirmation.
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Myosin is the main contractile protein of the muscles. Crystalline myosin could be Prepared in the form of needle crystals. The different rearrangements of such needles together may forming different descriptive shapes which may be used for meat identification of bird species. Three fresh thigh muscles from each species of the five studied species of birds were homogenized for preparation of their crystalline myosins. The results indicated presence of nine different descriptive shapes in the studies species of birds, the (most) characteristic shapes and their percentages were recorded for each species as following : for Fattening broiler chickens : Large thick needle - like crystals (18.9%) and contacted myosin crystals (5.22%), for Native broiler chickens: Branched point - like crystals (5.93%), large thick needle - like crystals (14.23%)and Contacted myosin crystals (8.51%), for Pigeons : Long branched stem - like crystals (16.97%), Short branched stem- like crystals (21.86%), for Ibises : X - litter shape - like crystals, (5.01%) and Contacted myosin crystals (15.93% ), and for Ducks : Frond shape - like crystals (3.57%), K - litter shape - like crystals (6.85%), and Short branched stem - like crystals (20.06%). For more improvement of such method for further confirmation of species, it could be suggested that the myosin ( crystals, solutions, molecules and subfraqment -1-crystals) should be studied by different ways to understanding the species differences in their (total compositions and amino acids either contents or sequences ) in the presence of fixed in vivo and in vitro factors, Also, the negative staining with fixation of different crystalline myosins for electron microscopical study and the x- ray diffraction patterns analysis on myosin crystals and the crystals of myosin subfragment- 1 should be studied for further confirmation.

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