Search PubMed⌕ Search

Biomedical subjects

K Worowski

Publications and source records attributed to K Worowski.

At least 163 records · Page 9Linked to original sources
PubMedDate not supplied

[Histopathological evaluation of protective effect of L-cysteine in ethanol-induced liver damage in rats].

Rats fed standard diet were intoxicated during 4 weeks with ethanol at the dose of 0.6 g/100 g of the body weight. This poisoning causes vacuolar degeneration, disappearance of glycogen granules, steatosis of hepatocytes and focal necrosis changes in the liver. The intake of food with cysteine at the dose of 0.012 and 0.024 g/100 g/24 hrs markedly prevents histopathological changes in the liver of rats intoxicated with ethanol. Larger amounts of cysteine (0.044 g/100 g/24 hrs) intensify histopathological changes caused by ethanol in the liver of rats.

Alcohol Deterrents↗
PubMedDate not supplied

Low molecular organic inactivators in differentiating organ origin of alpha-amylase in humans. Part I.

Alpha-amylases derived from pancreatic juice, saliva and granulocytes show different sensitivity to the low molecular organic inactivators. Pancreatic alpha-amylase is more susceptible to inhibitory activity of d-glyceraldehyde and d-mannitol and glycerol in comparison to alpha-amylase from saliva and granulocytes. Iodoacetate and urea exhibited inhibitory activity against granulocytic alpha-amylase and only a minute inactivation of salivary and pancreatic alpha-amylases was found. The most effective inhibition against all tested alpha-amylases was noted with dihydroxyacetone. We should stress, no evident differences were noted in the degree of sensitivity to this inactivator of the tested enzymes. The presumable mechanism of the inactivation of alpha-amylases with low molecular organic inactivators is briefly discussed. The procedure for the differentiation of organ origin of alpha-amylases is suggested.

Dihydroxyacetone↗
PubMedDate not supplied

[Inhibition by ethanol and acetaldehyde the plasmin activity and plasminogen activation induced by urokinase and streptokinase].

Ethanol and in a greater degree acetaldehyde inhibit activation of plasminogen evoked by urokinase and streptokinase. Ethanol does not inhibit the plasmin caseinolytic and fibrinolytic activities though the former inhibits amidolytic activity of the enzyme but only insignificantly. Acetaldehyde inhibits the plasmin activity towards casein, fibrin and H-D-Val-Leu-Lys-pNA.

Acetaldehyde↗
PubMedDate not supplied

[Effect of alcohols and the products of their oxidation on the fibrinolytic activity of euglobulins].

Aldehydes (formaldehyde and acetaldehyde) inhibit the fibrinolytic, caseinolytic and amidolytic activity of blood plasma euglobulins. Alcohols (methanol, ethanol, propanol and iso-propanol) and sodium salts of organic acids (formate, acetate and propionate) show inhibitory activity towards the fibrinolytic activity of euglobulins only at small degree and at high concentrations.

Alcohols↗