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Biomedical subjects

K Nowak

Publications and source records attributed to K Nowak.

At least 73 records · Page 4Linked to original sources
PubMed1983

Specificity of acid protease from Fusarium moniliforme.

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 three bonds: His(10)-Leu(11), Leu(11)-Val(12) and Tyr(26)-Thr(27) in oxidized beta chain of insulin.

Amino Acid Sequence↗
PubMed1981

Isolation and identification of the cyanogen bromide peptides of D-glyceraldehyde-3-phosphate dehydrogenase from human muscle.

D-Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from human muscle was S-carboxymethylated, cleaved with cyanogen bromide and citraconylated. The enzymatic protein contains 344 amino acid residues, nine of which are methionines. The respective ten cyanogen bromide fragments have been isolated and characterized. Each peptide was purified to homogeneity by Bio-Gel chromatography, high voltage electrophoresis and descending paper chromatography, and characterized by electrochromatography, N-terminal sequence and amino acid composition.

Chromatography, Gel↗
PubMed1981

Glyceraldehyde-3-phosphate dehydrogenase from human muscle: cleavage of tryptophanyl peptides with o-iodosobenzoic acid.

The new procedure of protein fragmentation with o-iodosobenzoic acid (Mahoney & Hermodson, 1979; Biochemistry, 18, 3810-3814) was used to split three tryptophanyl peptide bonds in glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from human skeletal muscle. The mixture obtained was separated into four homogeneous peptides by a one-step chromatographic procedure. High specificity of the cleavage reaction was proved by the amino acid analysis and determination of the N-terminal sequence of the peptide products. Both specificity ahd high yield obtained by this procedure confirmed its utility in the establishment of the protein primary structure.

Amino Acids↗
PubMed1981

Glyceraldehyde-3-phosphate dehydrogenase from human muscle: primary structure.

The complete sequence of 334 amino acids of glyceraldehyde-3-phosphate dehydrogenase (GPDH) from human muscle was established through the analysis of tryptic digests of the enzyme treated alternatively with bromocyanate, o-iodosobenzoic acid and maleic acid. Comparison of the primary structure of the enzyme from human muscle with that of the other known GPDH showed high homology; the closest similarity of the amino acid sequence was found between the enzymes from human and pig muscle.

Amino Acid Sequence↗
PubMed1981

The structure/activity relationship in glyceraldehyde-3-phosphate dehydrogenase of pig muscle.

The macromolecular digestion product obtained on limited proteolysis of glyceraldehyde-3-phosphate dehydrogenase (GPDH, EC 1.2.1.12) was fractionated into seven polypeptides. Their position in the known sequence of GPDH was established. The sites of chymotrypsin action at Phe-34, Tyr-91, Val-116, Leu-154, Leu-221 and Leu-246 were identified on the basis of N-terminal sequence and molecular weight of the peptides isolated. Cleavage of particular peptide bonds was related to the enzymatic activity.

Amino Acid Sequence↗
PubMed1981

A predicted secondary structure of protein protease inhibitors.

Basing on the Chou & Fasman method (Biochemistry, 13, 222-245; 1974) and the known amino acid sequences, the alpha-helical, beta-sheet, beta-turn and random-coil regions were predicted for protein protease inhibitors. It appears that in all the inhibitors examined there is a region conserved in the vicinity of the active site, composed of one beta-turn with an adjacent beta-sheet structure, and a second beta-turn situated in the other part of the polypeptide chain and linked with the first one by disulphide bridge. Two disulphide bridges between Cys2 and Cys25, and between Cys10 and Cys21 were proposed for the squash seed inhibitor. It is suggested that the two beta-turns play an essential role in the process of trypsin inhibition by protein protease inhibitors.

Amino Acid Sequence↗
PubMed1981

Homology of the predicted secondary structures of the N-terminal fragments of preproteins.

Secondary structures of the N-terminal fragments of 18 preproteins were analysed taking advantage of the method of Chou & Fasman (Biochemistry, 1974, 13, 222-245; J. Mol. Biol., 1977, 115, 135-175) and the known sequences of amino acid residues. Positions of alpha-helices, beta-sheet structures and beta-turns in the linear primary structure of preproteins have been proposed. Also it has been suggested that the three-dimensional structures of the N-terminal fragments of preproteins are homologous, irrespective of the differences in their primary structures, length of polypeptide chains, and function. A three-dimensional model of the N-terminal fragment is given, comprising the regions responsible for transport and removal of the signal peptide from preprotein. The location of prelipoprotein region responding to signal protease, and the substrate spatial requirements of this enzyme have been hypothesized.

Amino Acid Sequence↗
PubMed1980

Isolation and partial amino acid sequence of the trypsin inhibitor from the seeds of Cucurbita maxima.

Trypsin inhibitor from squash (Cucurbita maxima) seed was extracted with 0.1 M-acetate buffer, pH 4.5, purified on immobilized trypsin, and separated by SE-Sephadex C-50 chromatography into three active fractions. All of them inhibited trypsin to the same extent, showed no antichymotrypsin or antikallikrein activity, had a similar molecular weight (about 3300), and contained no tryptophan, phenylalanine or threonine. The partial amino acid sequence of tryptic and peptic peptides of fraction III was determined by Edman degradation procedure.

Amino Acid Sequence↗