Journal of Aquatic Food Product Technology · 2012 · 21 citations · 45 references
Life SciencesBiochemistryMolecular BiologyBone MetabolismStructural BiochemistryStructural BiologyBone Matrix CompositionBone PhysiologyBone TissueConnective TissueExtracellular MatrixCollagen BiologyFibersFourier TransformMolecular Architecture Of CollagenPh DependencePhase Transition TemperatureTriple Helix Structure
Acid-soluble collagen (ASC) was isolated from Pacific cod (Gadus macrocephalus) bone. The ASC was rich in glycine. The amount of imino acid was lower than that of calf skin collagen, as was the transition temperature (48.6°C). Electrophoresis revealed two different α chains (α1 and α2), β-component, and γ-component. Fourier transform infrared spectroscopy measurement showed that ASC was in triple-helix structure. ASC had a solubility greater than 90% in a very acidic pH range (pH 1–4), and the solubility decreased with increasing NaCl concentrations up to 3%. Lyophilized ASC had a network ultrastructure with lace-like fibers, similar to calf skin collagen sponge.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations