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The labelling of erythrocyte spectrin in situ with the hydrophobic reagent phenylisothiocyanate (Sigrist, H. and Zahler, P. (1978) FEBS Lett. 95, 116-120) is studied. Spectrin isolated from erythrocytes which have been incubated with phenylisothiocyanate is covalently modified by the probe. The modification in the spectrin molecule is stable under an excess(More)
1. The amino acid compostion, N- and C-terminal amino acid sequences, and the subunit molecular weight of glyceraldehyde phosphate dehydrogenase from human muscle, were determined. The obtained results and the maps of tryptic peptides suggest that the enzyme is composed of four identical or very similar polypeptide chains. 2. From the tryptic digest of(More)
Labelling of spectrin with the hydrophobic probes 2-naphthylisothiocyanate and 4-[125I]-iodophenylisothiocyanate dispersed in lipid vesicles was studied. Although spectrin is a peripheral protein of the erythrocyte membrane, it was found to be labelled as a result of incubation of washed red blood cells with hydrophobic arylisothiocyanates.
The amino acid sequences of tryptic peptides from the performic acid-oxidized trypsin inhibitor were determined. The degradation was performed with a new reagent, 3-isothiocyanato-4-methoxy-4'-nitrostilbene, and compared with the dansyl-Edman technique. The amino acid sequence of the trypsin inhibitor from bovine splenic capsule was found to be the same as(More)
Specificity of acid protease from Fusarium moniliforme was investigated using beta chain of oxidized insulin. The enzyme is highly specific for the bonds involving aromatic and hydrophobic amino acid residues. It shows high affinity for the following bonds: Leu(15)-Tyr(16), Tyr(16)-Leu(17), Phe(24)-Phe(25), Phe(25)-Tyr(26), and somewhat lower for other(More)
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