Abstract
The trypsin-inhibiting capacity of male adult mouse plasma was several-fold greater than that of the corresponding human plasma. Two major trypsin inhibitors were isolated from mouse plasma in an apparently homogeneous state. One seems to be homologous to alpha-1-antitrypsin isolated from several mammalian species, while the other, tentatively named contrapsin, does not correspond to any of the known plasma protease inhibitors that have been well characterized in human or other animals. When human plasma was fractionated in exactly the same fashion, no inhibitor corresponding to contrapsin was detected, suggesting the absence of this inhibitor in human plasma. No cross-reactivity was observed either between contrapsin and antiserum specific for alpha-1-antitrypsin or between alpha-1-antitrypsin and antiserum specific for contrapsin. alpha-1-Antitrypsin inhibited three serine proteases tested, i.e. porcine elastase, bovine trypsin, and chymotrypsin, whereas contrapsin inhibited only trypsin, but not the other two. The two inhibitors, however, shared a number of other properties in common. They were monomeric glycoproteins having total carbohydrate content of 9.6% in alpha-1-antitrypsin (Mr = 53,000) and 15.1% in contrapsin (Mr = 55,000). They had similar amino acid and carbohydrate compositions. They inhibited bovine beta-trypsin by forming stable complexes. They showed similar sex differences in blood concentrations. Serum levels of alpha-1-antitrypsin and contrapsin in males were 5.2 +/- 0.6 and 2.8 +/- 0.2 mg/ml, respectively, whereas those in females were 3.5 +/- 0.2 and 2.1 +/- 0.4 mg/ml, respectively.
Highlights
The trypsin-inhibiting capacity of male adult mouse relation between a-1-antitrypsin deficiencyand thepathogenplasma was several-fold greater than that of the cor- esis of these disorders, and further studies have been hamresponding human plasma
Since many tors were isolated from mouse plasma in an apparently inbred strains are available, the mouse seems suitable for homogeneous state
Amino Acid and Carbohydrate Compositions-The chemical compositions of mouse a-1-antitrypsin and contrapsin, and human a-1-antitrypsin are shown in Table 11.The values for human a-1-antitrypsin are in good agreement with those of the previous studies [5,6,7,8,9]
Summary
Teases such as chymotrypsin, elastase, plasmin, and thrombin [1]. Plasma levels of a-1-antitrypsin increase in theacute. The terminology of protease inhibitor is very confusing, and nostic and prognostic assessments. The mechanism of this at present there are many antiproteases which belong to entirely induced elevation is, still poorly understood. More than 20 genetic variants of human a-1-antitrypsinare reported to date, and a few alleles are shown to produce phenotypes with very low concentrations in plasma These phenotypes are associated with many chronic disorders in childhood, e.g. pulmonary emphysema, liver cirrhosis, glomerulonephritis, different categories in their chemical nature. Amino acid andcarbohydrate compositions of human andmouse a-I-antitrypsin, andmouse contrapsin. Experimental details for the determinations of amino acid and carbohydrate compositions were described previously [16].
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