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

100%

Minkiewicz I., Gindzienski A.

Acta Biochimica Polonica

1999

tom 46

nr 4

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.

Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella

100%

Kolodziejczyk R., Dobryszycki P., Ozyhar A., Kochman M.

Acta Biochimica Polonica

2001

tom 48

nr 4

The hemolymph juvenile hormone binding protein (JHBP) from Galleria mellonella contains two disulphide bridges/molecule and no free Cys residues. An alignment of primary structures of other Lepidopteran JHBPs indicates that Cys residues, equivalent to Cys10,17,151,195 in G. mellonella JHBP, may be involved in -S-S- bridge formation.

Ograniczanie wyników

2 Acta Biochimica Polonica

1 Dobryszycki P.

1 Gindzienski A.

1 Kochman M.

1 Kolodziejczyk R.

1 Minkiewicz I.

1 Ozyhar A.

1 2001

1 1999

Wyniki wyszukiwania

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

Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella