Molecules myofibrillar

Animal proteins, such as milk casein, whey, albumin, collagen, gelatin, keratin, and myofibrillar, are also proposed as raw materials to form edible films (13-15). Extended stmctures formed by unfolding of protein molecules are required for film formation. Amorphous three-dimensional stmctures formed by noncovalent interactions among protein chains stabilize the films. At high water content, films are produced by casting of viscous solutions, and at low water content, films are produced by extmsion using thermoplastic properties of proteins (13). 

Protein ( histidine ) Methyltransferase. An enzyme which methylates histidine in proteins to give primarily 3-methylhistidine residues has been observed in myofibrillar protein and in the sarcoplasmic fraction of muscle homogenates (218). S-Adenosyl-L-methionine serves as the methyl donor for the enzyme. The enzyme has not been solubilized and purified. Very little is known about the substrate specificity of protein-(histidine) methyltransferase. Actins from a wide variety of species consistently contain one 3-N-methylhistidine residue per molecule (191, 219). It appears that myosin from white muscle contains two residues of 3-N-methylhistidine (one residue per heavy chain), whereas myosin from red muscle contains no 3-N-methylhistidine (220). The amino acid sequence around the methylated residue of rabbit skeletal muscle is (221) ... 

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