S. Rapoport, T. Schewe's Processing and Turnover of Proteins and Organelles in the PDF

By S. Rapoport, T. Schewe

ISBN-10: 0080231772

ISBN-13: 9780080231778

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Read Online or Download Processing and Turnover of Proteins and Organelles in the Cell. FEBS Federation of European Biochemical Societies: 12th Meeting, Dresden, 1978 PDF

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Additional info for Processing and Turnover of Proteins and Organelles in the Cell. FEBS Federation of European Biochemical Societies: 12th Meeting, Dresden, 1978

Sample text

Communs. 31, 845 (1968). H. K. A. Shafnitz, Distribution of rat liver albumin mRNA membranebound and free in polyribosomes as determined by molecular hybridisation, Proc. Nati. Acad. Sci. 74, 5397 (1977). 51 R. Craig et (13) (14) (15) (16) (17) (18) (19) (20) (21) (22) (23) (24) al. R. Denamur, Ribonucleic acids and ribonucleoprotein particles of the mammary gland, Lactation 1, 413 (1974). K. N. Campbell, Molecular aspects of milk protein biosynthesis, Lactation 4, 387 (1978). S. K. N. Campbell, Isolation and characterization of messenger ribonucleic acid species for guinea-pig milk proteins from free and membrane-bound polyribosomes, Biochem.

Carbohydrate occurs as Gal-Hylys and/or Glc-Gal-Hylys To date the complete primary sequence of an a chain from a single species has not been determined but a composite sequence for the alfl) chain is available from studies of residues 1-418 of rat skin al(l) and residues 419-1052 of calf skin αΐ(ΐ) (δ). Over 95 per cent of the amino acids are arranged in triplets of structure -Gly-X-Y- and at both N- and C-termini are short non-triplet sequences (telopeptides) which are the remnants of longer sequences found in the collagen precursor polypeptides.

E. G. E. Cheah this difference is not yet clear. Analyses of the extension peptides indicate that their amino acid composition is quite unlike that of collagen and more typical of globular proteins (ll,12); and particularly significant is their content of cysteine which is not found in the fibril monomer of collagen types I and II. Inter-chain disulphide bonds are located only in the C-terminal extensions of procollagen types I and II although intrachain disulphide bonding occurs in the N-terminal extensions.

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Processing and Turnover of Proteins and Organelles in the Cell. FEBS Federation of European Biochemical Societies: 12th Meeting, Dresden, 1978 by S. Rapoport, T. Schewe


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