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Biomedical subjects

E Kolb

Publications and source records attributed to E Kolb.

At least 199 records · Page 11Linked to original sources
PubMed1975

[Calcium, magnesium, phosphorus, chloride and glucose in the blood of cattle following intravenous infusion of solutions with various calcium and magnesium concentration aimed at improving the treatment of hypomagnesemia].

Recent findings on changes in the mineral content of tissues in bovine hypocalcaemia and hypomagnesaemia show the necessity of using different mineral solutions for the treatment and prevention of these conditions. Infusion of 2% CaCl2-6H2O with 10% MgCl2-6H2O and 5% glucose one after the other or in combination produced severe functional changes in cardiac activity and respiration. Recommended concentrations for treatment or prophylaxis of hypomagnesaemia were 10 g magnesium chloride and 2 g calcium chloride, or alternatively 12 g magnesium adipate and 5 g calcium gluconate, in 100 ml of distilled water (total dose 500 ml). This was well tolerated and it overcame the mineral deficiency in tissues.

Animals↗
PubMed1975

[Mineral content of various tissues in cattle. 4. Studies on dry matter, Ca, Mg, Na and K concentration in mucous membrane and muscle layer of various bovine gastrointestinal sections].

Samples of the following parts of the gastrointestinal tract were collected from 20 slaughter cattle: - oesophagus, reticulum, omasum, rumen, abomasum, duodenum, jejunum, ileum, colon (beginning and end). There were considerable differences in mineral content, related to the differing functions of each part. Forestomach mucosa contained high concentrations of Ca and Mg, attributable to accumulation and separation of mineral salts. In the three segments of small intestine there was generally more Mg than Ca, with high concentrations of Na and K. The tabulated results are intended to provide a basis for comparison with pathological states.

Animals↗
PubMed1975

[Alkaline phosphatase activity in blood serum, bile and urine of cattle and calves].

Mean values and the range of values for alkaline phosphatase activity in serum (expressed in units) were: - calves 909 (413-1445), bulls 325 (179-543) and cattle 131 (72 to 162). Differences between these groups were statistically significant. Values for bile were: - calves 416 (116-882), cattle 546 (145-1203), bulls 738 (108-1438) enzyme units; here there were no significant differences. Activity of the enzyme in urine was very low, mean values being 0.77 in calves, 0.39 in cattle and 1.69 in bulls; the differences between groups were statistically significant.

Age Factors↗
PubMed1975

[Properties and isoenzymes of acid phosphatase in erythrocytes and various tissues (kidney, liver, spleen, small intestine mucosa, testis, myocardial and skeletal musculature) of cattle].

The substrate that was split most rapidly by acid phosphatase was p-nitrophenylphosphate. Two peaks of activity were obtained at pH 4.6-4.8 and 5.1-5.4. The enzyme remained stable for a long time when refrigerated. It was inhibited strongly by urea and tartrate, and slightly by fluoride and L-phenylalanine. Mercaptoethanol elicited pronounced activation of the enzyme. Four different forms of isoenzyme, giving rise to 11 phenotypes, were identified. A suitable analytical technique was electrophoresis on polyacrylamide gel with phosphate-citrate buffer. Mean activity was 3.15 +/- 0.41 units per gramme of haemoglobin haemolysate. Some of the isoenzyme preparations showed considerable variation in activity. There was no change in enzyme activity after temporary hypomagnesaemia. Acid phosphatase activity was high in testis, kidney and intestinal mucosa; myocardium, liver and spleen showed moderate activity. Five isoenzymes were demonstrable in a starch column and six in PAA gel.

Acid Phosphatase↗
PubMed1975

[Studies on activity and properties of alkaline phosphatase in body fluids (plasma, serum, bile) and in various organs (kidney, liver, small intestine, bones) in cattle].

Behaviour of the alkaline phosphatase (AP) present in blood serum, blood plasma, bile and extracts of organs (kidney, liver, intestinal mucosa, bone) was studied under various conditions of incubation (after preliminary heat treatment and after addition of L-phenyl-alanine). AP in serum and bile from calves and bullocks was very heat labile and did not inhibit phenylalanine much. EDTA and citrate were active inhibitors of AP, and therefore blood samples containing these anticoagulants are unsuitable for enzyme investigations. Out of four compounds tested, the substrate that was most rapidly split by AP from tissues was disodium phenylphosphate. AP activity was particularly high in kidney. The most heat-labile form of AP was that present in bone. AP in different tissues was inhibited to different extents by phenylalanine.

Alkaline Phosphatase↗
PubMed1975

[The influence of enflurane (ethrane) on surface activity of the lung (author's transl)].

Enflurane (Ethrane), a new inhalation anesthetic, was examined for possible surfactant alterating properties. To elucidate this question two groups of rabbits underwent investigation: the first group (5 animals) was mechanically ventilated with room air over a five hour period. In the second group (7 animals) for the same period Enflurane in clinical dosages was added the inspired gas. At the end of the procedure in neither group could signs of impaired lung surface activity be detected: All rabbits showed normal blood gas values, normal pressure volume diagrams and physiologic behaviour of lung extracts in the wilhelmy balance. We conclude first that artificial ventilation "per se" does not harm lung surfactant and second that Enfluran anesthesia is a good choice for outstanding long procedures as well as for patients with already impaired surface activity of the lung, because there seems to be little risk of aggravating the situation.

Animals↗
PubMed1975

[Activity and properties of adenosine triphosphatase in erythrocytes and various tissues (brain, liver, kidney, small intestine mucosa) of cattle].

In 15 samples of haemolysate of bovine erythrocytes, the splitting of phosphate from adenosine triphosphate average 158 +/- 63 X 10(-3) muMol/min/g haemolysate haemoglobin. Estimation of total adenosine triphosphatase in homogenates of various organs from cattle showed that spleen, liver, kidney and brain possessed high activity, while the activity was moderate in lung, myocardium and skeletal muscle, and low in endometrial mucosa and spinal cord. There was a relatively large proportion of Na-K-adenosine triphosphatase in brain and kidney. In various organs the activity of the enzyme was dependent upon the concentrations of Mg, Na, K and Ca. The inhibition of adenosine triphosphatase in various tissues by ouabain was studied. The optimum pH for the enzyme lay in the weakly alkaline region.

Adenosine Triphosphatases↗
PubMed1975

[Activity and properties of alkaline phosphatase in the plasma and various organs (kidney, liver, small intestine mucosa, bone) of the swine].

There was a high activity of alkaline phosphatase in the blood plasma of piglets during the first few days of live; enzyme obtained at this time had high heat stability and was readily inhibited by L-phenylalanine (5 mM). The enzyme in blood was inhibited to a greater extent than alkaline phosphatase from intestinal mucosa. With increasing age there was a fall in heat stability and in the ease with that the enzyme could be inhibited by phenylalanine. The proportion of alkaline phosphatase derived from bone and present in blood plasma increased with increasing age. Two isoenzymes were detected in liver, kidney, lung, intestinal mucosa and endometrial mucosa by electrophoresis in polyacrylamide gel. Heat lability and inhibition by phenylalanine were good criteria for differentiating different types of alkaline phosphatase in pigs. In the case of alkaline phosphatase in blood plasma, disodium phenylphosphate was split more readily than p-nitrophenyl phosphate and very much more readily than phenolphthalein diphosphate and beta-glycerophosphate.

Age Factors↗
PubMed1975

[Studies on the properties of acid erythrocyte phosphatase in sheep and the isoenzymes of sheep and goat acid erythrocyte phosphatase].

Ovine erythrocytic acid phosphatase showed two peaks of activity at pH 5.0 and 5.7 in acetate buffer with p-nitrophenylphosphate as substrate. The enzyme was only slightly inhibited by fluoride and L-phenylalanine, but high concentrations of urea strongly inhibited it. Activity of the enzyme was greater in goat erythrocytes than in sheep. By means of starch electrophoresis, three isoenzymes belonging to nine types were separated from the ovine enzymes, while three isoenzymes of five types were present in goats. Electrophoresis in polyacrylamide gel was suitable for detecting the rapidly migrating isoenzymes.

Acid Phosphatase↗
PubMed1974

Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material.

The preparation and purification of cyanogen bromide fragments from [(14)C]carboxymethylated coelacanth triose phosphate isomerase is presented. The automated sequencing of these fragments, the lysine-blocked tryptic peptides derived from them, and also of the intact protein, is described. Combination with results from manual sequence analysis has given the 247-residue amino acid sequence of coelacanth triose phosphate isomerase in 4 months, by using 100mg of enzyme. (Two small adjacent peptides were placed by homology with the rabbit enzyme.) Comparison of this sequence with that of the rabbit muscle enzyme shows that 207 (84%) of the residues are identical. This slow rate of evolutionary change (corresponding to two amino acid substitutions per 100 residues per 100 million years) is similar to that found for glyceraldehyde 3-phosphate dehydrogenase. The reliability of sequence information obtained by automated methods is discussed.

Amino Acid Sequence↗