The Effects of Strontium and Calcium on Mammalian Collagenases
Collagen is the major structural protein of skin, bone, cartilage, tendon, and teeth. It is, in fact, the most abundant protein in the body. The collagen molecule consists of three polypeptide chains, molecular weight approximately 95,000 each, which are coiled together in a triple helix. Chemically, the collagen molecule is unique in that every third amino acid residue is glycine, and in that it contains relatively large amounts of hydroxyproline and hydroxylysine.
KeywordsOrgan Culture Human Skin Collagen Molecule Epidermolysis Bullosa Human Skin Fibroblast
Unable to display preview. Download preview PDF.
- 1.J. Gross, Aspects of the animal collagenases, in: Biochemistry of Collagen (G. M. Ramachandran and A. H. Reddi, eds.), pp. 275–318, Plenum Press, New York (1976).Google Scholar
- 5.J. L. Seltzer, J. J. Jeffrey, and A. Z. Eisen, Evidence for mammalian collagenases as zinc ion metalloenzymes. Biochim. Biophys. Acta 485, 179–187 (1977).Google Scholar
- 6.H. Matsubara and J. Feder, Other bacterial, mold, and yeast proteases, in: The Enzymes (P. D. Boyer, ed.), Vol. 3, pp. 721–795, Academic Press, New York (1971).Google Scholar
- 12.J. D. McConn, D. Tsuru, and K. T. Yasunobu, Bacillus subtilis neutral protease I-A zinc enzyme of high specific activity. J. Biol. Chem. 239, 3706–3715 (1964).Google Scholar
- 13.E. A. Stein and E. H. Fischer, The resistance of α-amylases towards proteolytic attack. J. Biol. Chem. 232, 867–879 (1958).Google Scholar
- 14.A. Hasegawa and K. Imahori, Studies on α-amylase from a thermophilic bacterium. II. Thermal stability of the thermophilic α-amylase. J. Biochem. 79, 469–477 (1976).Google Scholar
- 15.M. R. Pollock, Exoenzymes, in: The Bacteria (E. C. Gunsalus and R. Y. Stanier, éds.), Vol. 4, pp. 121–178, Academic Press, New York (1962).Google Scholar
- 17.H. Ogawa and L. Goldsmith, Human epidermal’transglutaminase. Preparation and properties. J. Biol. Chem. 251, 7281–7288 (1976).Google Scholar