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Biomedical subjects

K Ohlsson

Publications and source records attributed to K Ohlsson.

At least 271 records · Page 15Linked to original sources
PubMed1976

Inhibitors of acrosin and granulocyte proteinases from human genital tract secretions.

Human seminal plasma contains two acid-stable proteinase inhibitors, HUSI-II (Mr approximately 6500) and HUSI-I, (Mr approximately 11 000) with different inhibition specificities. The inhibitory activity of HUSI-II is strongly limited to trypsin and acrosin; both enzyme-inhibitor complexes are very stable (e.g. bovine trypsin-HUSI-II complex: Ki = 1 x 10(-10)M; human acrosin-HUSI-II complex: Ki = 2.7 x 10(-10)M). The inhibitor from human seminal plasma HUSI-II may therefore be seen as the natural antagonist of the sperm protease acrosin. In addition to pancreatic trypsin and alpha-chymotrypsin, HUSI-I forms strong complexes with neutral proteases of the lysosome-like granules from human granulocytes, for example, the elastase (Ki = 2.5 x 10(-9)M) and cathepsin G, the chymotrypsin like protease (Ki = 7 x 10(-8)M).

Acrosin↗
PubMed1976

Inhibition of elastase from granulocytes by the low molecular weight bronchial protease inhibitor.

The low molecular weight bronchial protease inhibitor isolated from purulent bronchial secretions of man was shown to be a potent inhibitor of the elastase from human granulocytes. At a molar ratio of 1:1, the inhibitor prevented elastase digestion of insoluble elastin and soluble elastin, and blocked the hydrolysis of t-BOC-L-alanine-p-nitrophenyl ester. The collagenolytic activity of granulocyte collagenase was not inhibited by the bronchial inhibitor. Antisera were raised in rabbits for the isolation of specific IgG fractions in order to localize and quantitate the inhibitor. 125I-labelled inhibitor was used to study enzyme interactions further by gel filtration. These studies demonstrated that the bronchial inhibitor formed firm complexes with granulocyte elastase but did not form complexes with granulocyte collagenase.

Antibody Formation↗
PubMed1976

Radioimmunological determination and characterization of cathodal trypsin-like immunoreactivity in normal human plasma.

A radioimmunological method for determination of human cathodal trypsin-like immunoreactivity is described. DFP-treated human cathodal trypsin is used as standard and tracer. Freshly drawn normal human plasma contains about 25 microgram/l of cathodal trypsin-like immunoreactivity measured as DFP-treated cathodal trypsin. The normally circulating cathodal trypsin-like immunoreactivity is shown to consist mainly of cathodal trypsinogen.

Animals↗
PubMed1976

Purification of canine pancreatic secretory trypsin inhibitor and interaction in vitro with complexes of trypsin-alpha-macroglobulin.

Highly purified pancreatic secretory trypsin inhibitor (PSTI) from the dog was found to exist in three different chromatographic forms with equal capacities for the inhibition of trypsin. The molecular weight of the inhibitor, calculated from sodium dodecyl sulfate electrophoresis was approximately 7,000. It was capable of blocking proteolytic activity of trypsin-alpha-macroglobulin complex even though inhibition was never complete.

Animals↗
PubMed1976

Quantitation of active pancreatic endopeptidases in the intestinal contents of germfree and conventional rats.

Trypsin, chymotrypsin, and elastase were measured in the intestinal contents of germfree and conventional laboratory rats. Active trypsin was highest in the lower part of the small intestine and fell abruptly in the cecum. Trypsin was present in the feces of germfree rats but not of conventional laboratory rats. Electrophoresis of supernatant fluids from intestinal contents, and functional assays with specific synthetic substrates confirmed these results. The concentrations of active elastase were very high in the upper small intestine but low elsewhere. Active elastase was present in contents from the large intestine of germfree, but not conventional laboratory rats. These results suggest that normal microbiological inhabitants of the intestinal tract of rats play a role in the inactivation of pancreatic enzymes.

Animals↗
PubMed1976

Collagenase and elastase released during peritonitis are complexed by plasma protease inhibitors.

Peritoneal fluids from patients with diffuse peritonitis secondary to perforation of the appendix contained large quantities of collagenase and elastase. The enzymes, which existed in the form of complexes with plasma protease inhibitors, probably had been released from the granulocytes. The two enzymes had linked almost half of the alpha 1-antitrypsin and four fifths of the alpha 2-macroglobulin in the fluid. Evidence that regional defense against protease had failed was obtained by finding the C3 component of complement completely converted. Toxic peptides probably had been released. Recognition of plasma protease inhibitors as an important part of the regional defense against protease also suggested use for therapy. We lavaged the peritoneum postoperatively with fluid that did not contain plasma inhibitors but with volumes large enough to eliminate the accumulation of enzymes for the granulocyte.

Adult↗
PubMed1975

Granulocyte collagenase, elastase and plasma protease inhibitors in purulent sputum.

Sputum was collected from patients with purulent chronic bronchitis. Immuno-chemical techniques using rabbit antiserum against human granulocyte collagenase and elastase showed the presence of both enzymes. Also the serum protease ingibitors alpha1-antitrypsin and alpha2-macroglobulin were demonstrated. Their protease inhibiting capacity was saturated. Granulocyte elastase and collagenase occurred not only in complexes with the inhibitors, but also as free enzymes. All sputa showed free proteolytic, elastolytic and collagenolytic activity. The concentration of collagenase was equal in the sol phase and in the gel phase of the sputa, but most of the elastase was bound to the gel phase.

Alpha-Globulins↗
PubMed1975

Release of proteolytic enzymes in bile-induced pancreatitis in dogs.

Pancreatitis was induced by injection of autologous bile into the main pancreatic duct of dogs. An initial fall in blood pressure was accompanied by appearance of large quantities of active trypsin, chymotrypsin, and elastase in pancreatic exudate with full saturation of protease inhibitors. The enzymes soon appeared in ascitic fluid and lymph, but only in the form of complexes with alpha1-antitrypsin, and alpha2-macroglobulin. No such complexes were detected in venous blood indicating short half-life in the circulation. These studies confirm the release of pancreatic enzymes during bile-induced pancreatitis, and quantify an important protective role for plasma protease inhibitors in this situation.

Animals↗
PubMed1971

Isolation and immunochemical studies of dog trypsin.

Dog trypsin (EC 3.4.4.4) was isolated from dog pancreatic juice on SP-Sephadex C-50. The preparation was homogeneous on disc electrophoresis at pH 4.3. On agarose gel electrophoresis at pH 8.6, dog pancreas trypsinogen had the mobility of an alpha 2-globulin and trypsin the mobility of a beta-globulin. On gel filtration on Sephadex G-75 at pH 4.0, dog trypsin was eluted in the same fractions as bovine trypsin. It was inhibited by soybean trypsin inhibitor. Rabbit anti-dog trypsin inhibited the caseinolytic activity of bovine trypsin by about 60%.

Animals↗