Biomedical subjects
Publications and source records attributed to E Bańkowski.
Confluent cultures of Balb c/3T3, L-929 and PZ-32 cells were incubated at 37 degrees C for 16 h in the serum-free culture medium supplemented with ascorbic acid, beta-aminopropionitrile and (5(-3) H)proline. An addition of platelet homogenate to the culture medium increased significantly proline incorporation into proteins and synthesis of the hydroxyproline-containing, collagenase-sensitive proteins.
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Rat kidney fibroblasts transformed with SV-40 produce "in vitro" a significantly lower amount of hydroxyproline-containing material which is collagenase sensitive as compared to normal cells. In contrast to normal fibroblast cultures, no collagenous material was found by histochemical methods in intercellular spaces of transformed cultures.
The polymeric collagen of Guerin epithelioma is strongly bound to a large amount of noncollagenous substance. Almost full dissociation of this complex was achieved by heating in 7 Murea, at 100 degrees C for 4 hours. The collagen bound substance was identified as an acidic glycoprotein containing glucose, galactose, glucosamine, galactosamine and M-acetylneuraminic acid. Heterogeneity of this substance in regard to molecular weight was found.
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1. Digestion of procollagen I which trypsin, pepsin or pronase performed at 20 degrees C causes the release of acidic non-collagenous fragments and hydroxyproline-rich fraction. Enzymatic proteolysis performed at 41 degrees C (above the temperature of denaturation) results in degradation of procollagen I to low-molecular peptides. 2. The hydroxyproline-rich fraction obtained by limited proteolysis of procollagen I with pepsin (at 20 degrees C) contains a material corresponding to alpha and beta subunits of tropocollagen. Reduction of the hydroxyproline-rich fraction released by trypsin or pronase (at 20 degrees C) causes the appearance of polypeptides similar to pro-alpha subunits.
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The insoluble collagen from methylcholanthrene induced sarcoma was isolated and characterized. It contains more glycine, hydroxyproline and acidic amino acids than normal connective tissue collagen. An anionic character of tumour collagen was stated (pI 6.1). No typical collagen subunits in this protein were found. The tumour collagen is strongly bound to acidic glycoprotein containing a significant amount of hydroxylysine. Such an insoluble complex is resistant to the dispersing action of EDTA. It dissociates during heating in concentrated urea.
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1. The insoluble collagen from Guerin epithelioma was isolated and its chemical composition was determined. The unusually high histidine content is accompanied in tumour collagen by a relatively small amount of lysine and arginine. 2. The isolated protein was strongly bound to glycoprotein, which could not be removed by EDTA treatment unless this procedure was preceded by digestion of the complex with trypsin.
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