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ANALYSIS OF COLLAGEN FROM NORMAL AND ABNORMAL HUMAN BONE
Author(s) -
Quelch KJ,
Murphy WH,
Melick RA
Publication year - 1984
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1984.31
Subject(s) - cyanogen bromide , chemistry , guanidine , type i collagen , pyridinoline , polyacrylamide gel electrophoresis , amino acid , hydroxylysine , biochemistry , glycoprotein , medicine , peptide sequence , alkaline phosphatase , osteocalcin , enzyme , lysine , gene
Summary Using cyanogen bromide digestion of bone collagen, we have studied the type of collagen in normal bone, and in samples from patients with Paget's disease of bone, osteomalacia, osteoporosis and renal osteodystrophy. Despite extensive extraction with ethylene diamine tetraacetic acid and guanidine hydrochloride, not all of the glycoproteins could be removed from bone collagen. Upon electrophoresis on sodium dodecyl sulphate polyacrylamide gels, the cyanogen bromide peptides of insoluble bone collagen showed the pattern of type I collagen only in all samples, both normal and abnormal. Amino acid composition of the insoluble collagens and the ratio of hydroxylated and non‐hydroxylated amino acids were similar for all adult bone samples. These results suggest that the type of collagen in bone is not altered in the bone diseases examined.