ABSTRACT
The results of Pi typing by high resolution isoelectric focusing on 1,030 Normans from the area of Rouen (France) is reported. The frequency of the three common subtypes of Pi M is given and new variants partly described. Pi gene frequencies are compared to previously obtained data and results from other countries. The application of high resolution isoelectric focusing to the Pi system is discussed together with the advantages it provides in the knowledge of alpha-1-antitrypsin genetic polymorphism.
Subject(s)
Genetic Variation , Phenotype , alpha 1-Antitrypsin/genetics , Female , France , Gene Frequency , Humans , Isoelectric Focusing , Male , alpha 1-Antitrypsin/analysisABSTRACT
Serum trypsin esterolytic activity was measured in 106 sera from 61 controls and 45 patients with pancreatitis. A trypsin specific synthetic substrate, N-alpha-benzoyl-L-arginine-paranitroanilide, was used. High levels of enzymatically active trypsin were shown to be present in serum of patients with pancreatitis. No difference between the two samples was noticed for the serum concentrations of alpha-1-antitrypsin and alpha-2-macroglobulin (the two main serum trypsin inhibitors). Active trypsin was contained in the high molecular weight fraction of plasma proteins, corresponding to a complex with alpha-2-macroglobulin. The determination of serum typsin activity as a sensitive test for detection of pancreatitis was demonstrated to be statistically significant.
Subject(s)
Pancreatitis/enzymology , Trypsin/blood , Adult , Aged , Alcoholism/blood , Alcoholism/complications , Benzoylarginine Nitroanilide/metabolism , Chromatography, Gel , Female , Humans , Male , Middle Aged , Pancreatitis/complicationsABSTRACT
Alpha-1-antitrypsin deficiency is responsible for emphysema in adults. The genetic polymorphism of this protein (Pi system) is used to detect these deficiencies. The relationship between the serum protease inhibitory capacities and M, MZ and Z Pi phenotypes was investigated. 120 sera including 31 M, 33 MZ and 56 Z were studied. The alpha-1-antitrypsin concentration varied according to the Pi phenotype, the sex and the health of the subject. The alpha-2-macroglobulin level did not depend on the Pi phenotype. The trypsin inhibitory capacity fluctuated with the age and the health of the subject, but did not faithfully represent the Pi phenotype. In contrast, the elastase inhibitory capacity depended only on the Pi phenotype. The relationship between alpha-1-antitrypsin levels and the serum elastase inhibitory capacities was linear. Canonical analysis was employed to determine the relative contributions of each antiprotease to the two inhibitory capacities. It appeared that the elastase inhibitory capacity was influenced more by the alpha-1-antitrypsin level while the trypsin inhibitory capacity was more sensitive to alpha-2-macroglobulin.
