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H Zuber

Publications and source records attributed to H Zuber.

At least 109 records · Page 6Linked to original sources

Carboxypeptidase C.

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Carboxypeptidases↗

The complete amino acid sequences of both subunits of the sweet protein monellin.

The amino acid sequences of both chains of the sweet protein Monellin have been determined. Since chain separation could not be accomplished easily, cyanogen bromide cleavage at the only methionine residue (in the B-chain) was performed and the three products obtained after cyanogen bromide cleavage were separated. For the identification of amino acid phenylthiohydantoins, high performance liquid chromatography was employed. Thus 37 out of a total of 44 residues of the A chain and 40 out of a total of 42 residues of the large CNBr fragment of the B chain could be determined after Edman degradation of the polypeptides on an automated sequenator.

Amino Acid Sequence↗

The function of the two subunits of thermophilic aminopeptidase I.

The thermophilic high-molecular-weight aminopeptidase I (EC 3.4.11.1) from Bacillus stearothermophilus is composed of 12 subunits of two different types (alpha,beta) which can combine in various ratios. Only one type of subunit (alpha) is needed for the degradation of neutral peptides, but dipeptides having amino-terminal aspartic or gultamic acid are substantially hydrolyzed only by enzyme containing the other subunit (beta) as well. Asp-Gly inhibits the enzymatic hydrolysis of glutamic acid 1-(4-nitroanilide) very strongly but hardly affects the hydrolysis of leucine p-nitroanilide. These results indicate that both types of subunit have hydrolytic activity but different specificity. The two subunits have identical molecular weights and their amino-terminal regions are homologous, suggesting that the two chains originate from a single ancestral gene by gene duplication and independent mutation.

Amino Acid Sequence↗