By Magne K. Fagerhol, Diane Wilson Cox (auth.), Harry Harris, Kurt Hirschhorn (eds.)
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Additional resources for Advances in Human Genetics 11
3 g/liter. , 1962), severe protein-losing conditions (Eriksson, 1965), and terminal liver failure (Talamo, 1975). In these conditions an increased consumption in association with decreased synthesis or release of the protein probably leads to decreased plasma levels. Talamo (1975) has also seen severe lowering of a (AT at some point during the course of cystic fibrosis in twelve out of 105 patients, but the mechanism remains obscure. , 1978), thiol proteinases (Johnson and Travis, 1977), and cigarette-smoke condensate (Janoff and Carp, 1977).
In the absence of inhibition, the proteolytic enzymes can digest elastin, collagen, microfibrillar component, and proteoglycans. , 1978). AT. A general model for inhibition of proteases, based upon studies of the interaction between trypsin and soybean trypsin inhibitor, was formulated by Laskowski et al. (1971). According to this model, the active site of the inhibitor contains either a single Arg-X or Lys-X bond. , 1971; Johnson and Travis, 1975). AT with enzymes suggests that the inhibitor site of cx.
These authors also showed that removal of sialic acid from the M protein resulted in an extremely rapid removal of a,AT from the circulation. Even a 20% desialylation doubled the fractional catabolic rate. , 1974). Concentration of