ABSTRACT
The review is devoted to sources of lipids in enteral and parenteral nutrition. The role of omega-3 and omega polyunsaturated fatty acids in metabolism of some lipid mediators is examined.
Subject(s)
Enteral Nutrition , Fatty Acids/metabolism , Lipids/chemistry , Parenteral Nutrition , Animals , Fatty Acids/chemistry , Fatty Acids, Omega-3/chemistry , Fish Oils , Humans , Lipid MetabolismABSTRACT
The effect of oxygen, structurally-binded with water (oxygen water), on electrical activity of rat jejunum in early postoperative period. It was shown, that in contrast to effect of 0.9% NaCl, there is normalization of electrical activity parameters (frequency and slow wave amplitude) of jejunum in early postoperative period under the influence of oxygen water.
Subject(s)
Action Potentials/drug effects , Antioxidants/pharmacology , Jejunum/physiology , Oxygen/pharmacology , Water/pharmacology , Action Potentials/physiology , Administration, Oral , Animals , Electrodes, Implanted , Ischemia/prevention & control , Jejunum/blood supply , Jejunum/surgery , Male , Models, Animal , Oxidative Stress/drug effects , Oxygen/chemistry , Postoperative Period , Rats , Rats, Wistar , Water/chemistryABSTRACT
The lipase (triglyceridase) and cholesterol-esterase activities were detected in the salivary gland secretions of medicinal leeches (Hirudo medicinalis). The specific activities of these enzymes were found to be equal to 8.2 +/- 0.3 and 3.1 +/- 0.2 nmol/mg of protein per hour, respectively. It was shown that the cholesterol esterase activity of the secretions is suppressed by 60% by sodium cholate.
Subject(s)
Carboxylic Ester Hydrolases/metabolism , Lipase/metabolism , Saliva/enzymology , Sterol Esterase/metabolism , Animals , Cholic Acid , Cholic Acids/pharmacology , Hydrolysis , Kinetics , Leeches , Salivary Glands/enzymology , Sterol Esterase/antagonists & inhibitors , Triolein/metabolismABSTRACT
Isolation of triglyceridase from pig aorta was carried out by means of a following procedure: preparation of acetone powder, extraction of the enzyme in presence of sodium deoxycholate, ammonium sulfate fractionation, chromatography on Sepharose 6B, DEAE cellulose and cholate-Sepharose. The 1,000-fold purification of the enzyme was achieved. The purified preparation of triglyceridase was free of cholesterol esterase and proteinase activities.
Subject(s)
Aorta/enzymology , Lipase/isolation & purification , Animals , Carbon Radioisotopes , Kinetics , Molecular Weight , SwineABSTRACT
Triglyceridase activity in porcine aorta extracts was determined by splitting of glycerol-tri-[1-14C]-oleate. On the basis of inhibition of the activity by sodium chloride and protamine sulfate, as well as on the basis of activation by apoproteins of high density lipoproteins, the occurrence of lipoprotein lipase in the aorta was demonstrated. The data obtained suggest that 60--80% of triglyceridase activity is due to lipoprotein lipase.
Subject(s)
Aorta/enzymology , Lipoprotein Lipase/analysis , Swine , Triglycerides/metabolism , Animals , In Vitro TechniquesABSTRACT
Cholesterol esterase was isolated from canine pancreatic juice by DEAE-cellulose and hydroxylapatite chromatography. The preparation obtained was free from detectable proteinase and lipase activity. The cholesterol esterase activity was increased by adding boiled pancreatic juice. This fact allowed a preliminary conclusion that pancreatic juice contains an activator of cholesterol esterase.
Subject(s)
Carboxylic Ester Hydrolases/isolation & purification , Pancreatic Juice/enzymology , Sterol Esterase/isolation & purification , Animals , Dogs , MethodsABSTRACT
The separation of catalytic cAMP-independent and regulatory cAMP-binding subunits of pigeon breast muscle protein kinase was performed after the treatment of the holoenzyme by cAMP. The molecular weight of the homogeneous catalytic subunit is determined as 30,000. When catalytic and regulatory subunits were mixed, the decrease of phosphotransferase activity was observed.
Subject(s)
Columbidae/metabolism , Muscles/enzymology , Protein Kinases/isolation & purification , Animals , Catalysis , Cyclic AMP , Macromolecular Substances , Molecular Weight , Protein Kinases/metabolismABSTRACT
Protein kinase was isolated from pigeon breast muscle. The preparation obtained was chromatographically homogeneous. The apparent Km varlue for histone H1 and ATP were 3,5-10(-5) M and 1,6-10(-5) M respectively. The purified enzyme displays high specificity for the lysine-rich histones (H1, H2b, H2a). The protein kinase activity is stimulated, 1,6-fold by cyclic AMP.
