𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Heat-Induced Gelation of Myofibrillar Proteins and Myosin from Fast- and Slow-Twitch Rabbit Muscles

✍ Scribed by C. BOYER; S. JOANDEL; V. ROUSSILHES; J. CULIOLI; A. OUALI

Book ID
108820922
Publisher
Institute of Food Technologists
Year
1996
Tongue
English
Weight
168 KB
Volume
61
Category
Article
ISSN
0022-1147

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Determination of Surface Hydrophobicity
Determination of Surface Hydrophobicity of Fast and Slow Myosins from Rabbit Skeletal Muscles: Implication in Heat-Induced Gelation
✍ Boyer, CΓ©cile; Joandel, Sandra; Ouali, Ahmed; Culioli, Joseph πŸ“‚ Article πŸ“… 1996 πŸ› John Wiley and Sons 🌐 English βš– 846 KB

Both aliphatic and aromatic surface hydrophobicities of myosins from fast-twitch psoas major and slow-twitch semimembranosus proprius muscles were investigated using fluorescence probes (cis-parinaric acid and 8-analino-l-naphthalene sulphonic acid). Surface hydrophobicity of unheated slow myosin wa

Heterogeneity of myofibrillar proteins i
Heterogeneity of myofibrillar proteins in lobster fast and slow muscles: Variants of troponin, paramyosin, and myosin light chains comprise four distinct protein assemblages
✍ Mykles, Donald L. πŸ“‚ Article πŸ“… 1985 πŸ› John Wiley and Sons 🌐 English βš– 883 KB

Fast and slow muscles from the claws and abdomen of the American lobster Homarus americanus were examined for adenosine triphosphatase (ATPase) activity and for differences in myofibrillar proteins. Both myosin and actomyosin ATPase were correlated with fiber composition and contractile speed. Four