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Biomedical subjects

H Grossmann

Publications and source records attributed to H Grossmann.

At least 55 records · Page 3Linked to original sources
PubMed1976

Further evidence for common antigens in intracytoplasmic A particles of mouse mammary tumors and B type virions of murine milk.

Using the indirect immunofluorescence technique and radioimmunoprecipitation test (RIP test) according to ABELEV and ELGORT (1970) immunological investigations intracytoplasmic A particles isolated from mouse mammary tumors were performed. In order to purify the virus particles sucrose gradients were employed according to TANAKA et al. (1972) and in some details according to SMITH and WIVEL (1973). In immunofluorescence studies on mammary tumor slices a complete cross-reaction between antisera against A particles from mammary tumors and MTV-B particles from mouse milk was observed. Both kinds of antisera reacted in identical fluorescence pattern types with intracytoplasmic A particle clusters and with extracellular accumulations of B type virions, respectively, in tumors of different histological structures. RIP test studies suggest that these cross-reactions are attributed to three common antigens in A and B type viruses. Thus, there does not remain any doubt that intracytoplasmic A particles in murine mammary tumors are MTV-related. All these A particles antigens were identically detected using an antiserum against A particles isolated from mouse leukemia cells (serum kindly provided by Dr. TANAKA). The biological role of intracytoplasmic A particles in mouse tissues is discussed. In contrast to the precursor theory, it is believed that they could represent something like a nonsense way of particle maturation in MTV-infected cells.

Animals↗
PubMed1976

[Serum protein changes in liver transplantation in the dog].

Hemorrhage and shock gave rise to quantitative determination of serum protein changes by means of the two-dimensional immunoelectrophoresis according to Laurell. 5 proteins showed significant changes. There were no new protein peaks or products of decomposition of other serum proteins. The liver injured by ischemia can not alone be responsible for the shift of serum proteins. Rather probably the majority of lost proteins remains in the splanchnic area.

Animals↗
PubMed1975

[The chemistry of a chitin-protein from crayfish (Astacus fluviatilis) (author's transl)].

A chitin-protein complex is obtained from crayfish (Astacus fluviatilis) by gentle decalcification with acetic acid and EDTA. The complex is treated with lithium rhodanide, urea, anhydrous formic acid, pronase, papain, anhydrous formamide or 1N NaOH. The first three of these substances have little or no effect on the stability of the chitin-protein complex. The enzymes remove most of the protein, and the last two reagents remove all of it. The protein remaining bound to the polysaccharide after treatment of the chitin-protein complex with pronase or papain is relatively rich in glycine. Quantitative analysis yielded values for the acetyl, glucosaminyl and amino acid residues which reproduce the composition of the corresponding chitin-protein complex. In these calculations however, allowance must be made for the fact that glucosamine is partly destroyed by the acid by hydrolysis and interferes with the determination of basic amino acids. The results of the present work suggest that the chitin in crayfish is present in the form of a stable complex with protein, possibly held together by covalent binding of the protein to the chitin, with glycine as the connecting amino acid.

Amino Acids↗
PubMed1975

[Purification of the acetylcholinesterase from human erythrocytes by affinity chromatography (author's transl)].

The acetylcholinesterase from human erythrocytes was released from the plasma membrane with 0.2% Triton X-100 at low ionic strength and purified by two affinity chromatography steps on Sepharose-bound m-[6-(6-amino-caproylamino)caproylamino]phenyltrimethyl-ammonium. The synthesis of the inhibitor is described. The purified, detergent-free acetylcholinesterase was obtained with a specific activity of 4270 U/mg (158000-fold purification) and a 28% yield. The enzyme is a glycoprotein and aggregates in the absence of Triton X-100 into higher molecular complexes. The molecular weight was estimated by sodium dodecylsulfate electrophoresis to be 80000 +/- 3000 in the presence of 2-mercapto-ethanol and 154000 +/- 6000 in its absence.

Acetylcholinesterase↗
PubMed1975

[Isolation of carcinoembryonic antigen].

A method employed in the authors' laboratory for isolating the carcinoembryonic antigen (CEA) from tumours of the entodermal digestive tract and their metastases is described. The main step is fractionation of the preparations obtained by perchloric acid extraction using gel filtration on Sephadex G-200, Sepharose 4 B, and Sepharose 6 B at pH 4.5 and 7.0. The peaks with CEA-specific antigeneity were characterized by the distribution coefficient of the CEA between the mobile and the stationary phases (Kav), and by the relative elution volume (ve/vo). The CEA purified by gel filtration could not reliably be enriched through preparative electrophoresis in Sephadex G-25 gel, polyacrylamide gel or Pevikon powder. The isolation procedures used were compared with those reported in the literature, and the results obtained are discussed.

Adult↗