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Biomedical subjects

H J Horstmann

Publications and source records attributed to H J Horstmann.

8 recordsLinked to original sources
PubMed1977

Congenital dyserythropoietic anaemia, types I and II: aberrant pattern of erythrocyte membrane proteins in CDA II, as revealed by two-dimensional polyacrylamide gel electrophoresis.

The protein composition of the erythrocyte membrane of two patients with CDA I and four patients with CDA II has been investigated by two-dimensional polyacrylamide gel electrophoresis. The two-dimensional patterns of erythrocyte membrane proteins of the patients with CDA were compared with the well-established pattern of normal individuals. No alterations could be detected in the patients with CDA I, but a striking deviation from normal was observed in all patients with CDA II. The major aberrations of the erythrocyte membrane proteins in CDA II are the lack of protein B1.1, the drastically increased concentration of protein B1.4 and the presence of a new component, C2'. These results are discussed in relation to the known morphological and immunological abnormalities of the erythrocyte membrane in CDA II.

Anemia↗
PubMed1977

Macroamylasaemia after treatment with hydroxyethyl starch.

After infusion of 500 ml of 6% hydroxyethyl starch into fifty-four patients an increase of serum amylase was observed which in fifty-one cases exceeded the upper limit of normal (190 U/l). In most cases serum amylase reached twice the basal value. Renal function influenced the duration of the increase in serum amylase, but not the maximum increase (201+/-15 U/l; mean+/-SEM). In patients with advanced renal failure (glomerular filtration rate (GFR) = 2-10 ml/min) serum amylase was still markedly elevated after 72 h (298+/-24 U/l; mean+/-SEM). In patients with normal renal function (GFR greater than 90 ml/min) serum amylase decreased to 183+/-40 U/l (mean+/-SEM) within 72 h without reaching basal values. After infusion of HES no changes were observed in serum lipase or in amylase or lipase activities in duodenal secretion. Amylase excretion in the urine decreased. The assumption of a macroamylasaemia caused by formation of an HES-amylase complex was confirmed by gel filtration. The elimination from plasma of this high molecular enzyme-substrate complex is slow and causes hyperamylasaemia. In no case was the macroamylasaemia associated with signs or symptoms. An awareness of this causal relationship seems to be important, to avoid the erroneous diagnosis of a pancreatic disease.

Adult↗
PubMed1977

Hydroxyethyl starch-induced macroamylasemia.

Summarizing, the following results were obtained: 1. After infusion of 500 ml hydroxyethyl starch 6% in all patients an increase of serum amylase occurred, which in most cases reached values twice as high as the basal value. 2. This hyperamylasemia is caused by the formation of a high molecular HES-amylase complex, which cannot be easily eliminated. 3. In no case was hyperamylasemia associated with other clinical signs or symptoms.

Amylases↗
PubMed1977

[Formation of high-molecular aggregates between serum amylase and colloidal plasma substitutes (author's transl)].

The distribution of molecular weights of human serum amylase was studied by gel filtration of serum, obtained before and after infusion of the colloidal plasma substitutes hydroxyethyl starch, dextran and gelatin, respectively. Both in serum, drawn after intravenous infusion of hydroxyethyl starch, and in a solution of hydroxyethyl starch with serum we observed a significant increase in the molecular weight of serum amylase. The occurrence of this "macroamylase" may be explained by the formation of aggregates between hydroxyethyl starch and amylase. Because of its high molecular weight the elimination of this, presumably, enzyme-substrate-complex is retarded, thus leading to the observed increase of serum amylase activity. In contrast to these observations concerning hydroxyethyl starch no change in the apparent molecular weight of serum amylase was observed following the infusion of either gelatin or dextran or their solutions with serum.

Amylases↗
PubMed1975

Two-dimensional polyacrylamide-gel electrophoresis of the proteins and glycoproteins of the human erythrocyte membrane.

A two-dimensional polyacrylamide gel electrophoresis technique has been developed, improving the analytical separation of some proteins and glycoproteins of the human erythrocyte membrane. Freshly prepared membranes are totally solubilized, subjected to dodecylsulfate--polyacrylamide gel electrophoresis in the first dimension, followed by electrophoresis in the second dimension, using a detergent-free polyacrylamide gradient gel. By this method the proteins of the human erythrocyte membrane could be resolved into a two-dimensional pattern, which has been shown to be highly reproducible with respect to various blood-groups and within one blood-group from specimen to specimen. The method enables especially the investigation of the hydrophobic and very likely integrated membrane proteins and glycoproteins. Thus, band III[Fairbanks, G., Steck, Th. & Wallach, D. F. H., Biochemistry, 10, 2606--2617 (1971)] could be shown to consist of five proteins, one of them being the major glycoprotein of the human erythrocyte membrand. The two spectrin bands differed considerably in their two-dimensional patterns. The value of the given method for the investigation of membrane defects, which may be linked with various diseases of human erythrocytes, could be demonstrated in the case of two patients suffering from congenital dyserythropoetic anaemia.

Blood Proteins↗