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5 Acta Biochimica Polonica

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Low molecular mass products of depolymerization of purified mucin - attempts at isolation and characterization

100%

Minkiewicz I. , Gindzieński A.

nr 4

928-933

Samples of crude mucin were incubated at room temperature for 48 and 96 h in a sodium azide containing buffer, pH 7.0. Then each sample was purified, reduced and alkylated with iodo[^14C]acetamide. Electrophoretic analysis demonstrated that radioactivity was incorporated into the mucin subunits and proteins of 100 and 140 kDa. The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges.

Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.

80%

Galicka A. , Wołczyński S. , Gindzieński A.

nr 2

481-488

Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by L-[5-3H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30°C for 5 min generated a shorter than normal α2 chain which melted at 36°C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C→G causing a substitution of histidine by aspartic acid in the α2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-α1(I) form as compared with control cells.

EF-1α Is a target site for an inhibitory effect of quercetin in the peptide elongation process

80%

Marcinkiewicz C. , Gałasiński W. , Gindzieński A.

1995

tom 42

nr 3

347-350

Low molecular mass products of depolymerization of purified mucin - attemps of isolation and characterization

80%

Minkiewicz I. , Gindzieński A.

nr 4

929-933

Application of aqueous hydrazine solution for β-elimination of O-glycans from gastric mucin

70%

Kisiel D. , Gindzieński A. , Gadek A.

nr 3

753-757