Subject(s)
Bronchopulmonary Sequestration/diagnosis , Contrast Media , Image Enhancement , Magnetic Resonance Imaging/methods , Torsion Abnormality/diagnosis , Abdominal Pain/etiology , Arteries/abnormalities , Arteries/surgery , Bronchopulmonary Sequestration/surgery , Child , Diagnosis, Differential , Humans , Infarction/diagnosis , Infarction/surgery , Lung/blood supply , Male , Organometallic Compounds , Pleural Effusion/etiology , Surgical Instruments , Thoracic Surgery, Video-Assisted , Torsion Abnormality/surgery , Vomiting/etiologySubject(s)
Abdomen , Cerebral Palsy/diagnosis , Emergency Service, Hospital , Foreign Bodies/diagnosis , Hematemesis/etiology , Intellectual Disability/diagnosis , Intestines , Vomiting/etiology , Cerebral Palsy/complications , Child , Diagnosis, Differential , Humans , Intellectual Disability/complications , MaleABSTRACT
Platelets were isolated from blood donated by 57 diabetic subjects, 41 insulin-dependent and 16 non insulin-dependent, ranging in age from 19 to 78 years, and by 54 healthy non-diabetic subjects ranging from 19 to 63 years of age. The platelets were ruptured by sonication and resultant preparations assayed for their levels of activity of seven acid glycohydrolases. Platelets from diabetic subjects contained only 50% of the alpha-L-fucosidase activity and about 60% of the acid phosphatase, beta-D-galactosidase, and beta-D-glucosidase activities of platelets from non-diabetic individuals; the differences were statistically significant. N-acetyl-beta-D-glucosaminidase activity in platelets from diabetic subjects was reduced by about 15% from normal levels while beta-D-glucuronidase and alpha-D-mannosidase activities were similar to those from non-diabetic individuals. A comparison of the data from older insulin-dependent diabetic and normal subjects with a similar age distribution yielded identical results for the two groups in all enzymes tested except fucosidase. Platelets of non insulin-dependent diabetics and those from non-diabetic subjects of a similar age distribution appear to possess similar levels of these acid hydrolases. There was no difference in levels of these platelet acid hydrolases between males and females in either the diabetic or non-diabetic group. Within the diabetic group, there was no difference in these platelet acid hydrolase activities between subjects with retinopathy and without retinopathy. There was no correlation of the enzyme activity levels of platelets from diabetic subjects with concentration of glycosylated haemoglobin, serum triglycerides or serum cholesterol.
Subject(s)
Blood Platelets/enzymology , Diabetes Mellitus/enzymology , Glycoside Hydrolases/blood , Acid Phosphatase/blood , Adult , Aged , Female , Glycated Hemoglobin/metabolism , Humans , Male , Middle AgedABSTRACT
The production of 14CO2 from L-[1-14C]fucose and D-[1-14C]arabinose been studied in five mammalian species. Cats, guinea pigs, mice, and rabbits respired about 22% of the label of L-[1-14C]fucose or of D-[1-14C]arabinose within 6 h after intraperitoneal injection of the sugar. Rats respired only 1.5% of the L-fucose label and 5% of the D-arabinose label in the same time period. Liver homogenates from cat, guinea pig, and rabbit produced significantly more 14CO2 from L-[1-14C]fucose or D-[1-14C]arabinose than mouse or liver homogenates. Unlike those of the other species, guinea pig liver homogenates had very low L-fucose dehydrogenase activity. The results suggest that substantial catabolism of L-fucose and D-arabinose occurs in the tissues of some animal species. Investigators wishing to employ L-fucose as a tracer of glycoprotein metabolism must, therefore, ensure that the species that they employ does not metabolize L-fucose to products interfering with their studies.
Subject(s)
Arabinose/metabolism , Carbon Dioxide/metabolism , Fucose/metabolism , Respiration , Animals , Carbon Radioisotopes , Cats , Female , Glycoproteins/metabolism , Guinea Pigs , In Vitro Techniques , Liver/metabolism , Male , Mice , Rabbits , Rats , Species Specificity , Time FactorsSubject(s)
Carbohydrate Dehydrogenases , Amino Acids/analysis , Animals , Carbohydrate Dehydrogenases/analysis , Carbohydrate Dehydrogenases/antagonists & inhibitors , Carbohydrate Dehydrogenases/metabolism , Fucose , Isoelectric Point , Liver/enzymology , Macromolecular Substances , Molecular Weight , Osmolar Concentration , Sheep , Substrate SpecificityABSTRACT
1. The sorbitol dehydrogenases [L-iditol: NAD oxidoreductase] from livers of cow, man, rat and sheep each possess molecular weights of about 140,000. The beef, rat and sheep liver enzymes are composed of subunits of molecular weight 40,000. 2. The sorbitol dehydrogenases from livers of these four species each possess an isoelectric point of 7.3. 3. The four enzyme preparations show identical mobilities upon disc-gel electrophoresis and yield a single band of enzymic activity. 4. Sorbitol dehydrogenase activity is activated by the presence of ampholines or by increasing ionic strengths, with maximal activation at about 0.5 M salt concentration. These factors may cause the Km for NAD to be lowered.