muramidase has been researched along with 4-vinylpyridine* in 2 studies
2 other study(ies) available for muramidase and 4-vinylpyridine
| Article | Year |
|---|---|
Development of an acid hydrolysis method with high recoveries of tryptophan and cysteine for microquantities of protein.
High recoveries of tryptophan and cysteine were achieved by 12.5 min of hydrolysis with mercaptoethanesulfonic acid vapor. Proteins (1-100 micrograms) were modified by vapor-phase S-pyridylethylation before hydrolysis. The modified proteins were hydrolyzed with the vapor of 2.5 M mercaptoethanesulfonic acid at 176 degrees C. This method promoted efficient hydrolysis of the peptide bonds in proteins and resulted in high recoveries of both tryptophan and cysteine, of 90% or greater, in addition to the other amino acids. Topics: Acetates; Acetic Acid; Amino Acids; Chromatography, Ion Exchange; Cysteine; Hydrolysis; Microchemistry; Muramidase; Myoglobin; Ninhydrin; Proteins; Pyridines; Time Factors; Tryptophan | 1991 |
On-sequencer pyridylethylation of cysteine residues after protection of amino groups by reaction with phenylisothiocyanate.
Cysteine residues in polypeptides are not easily identified during automated N-terminal sequence analysis. Reaction of cysteine side chains with 4-vinylpyridine and identification as the pyridylethylated phenylthiohydantion derivative (PE-PTH-Cys) were proposed. However, after this reaction a desalting step is necessary. If limited sample amounts do not allow this desalting step, on-sequencer pyridylethylation is an alternative, although preview of the consecutive amino acid is usually observed in this case. We describe an on-sequencer procedure that avoids such preview formation by derivatizing the peptide with phenylisothiocyanate (PITC) prior to reaction with 4-vinylpyridine. The pyridylethylation is performed in the cartridge of the sequencer after immobilization of the protein or peptide on a polybrene-coated glass fiber filter and thiocarbamylation with PITC. Preview caused by N-alkylation is not observed and PE-PTH-Cys is detected in much higher yields than usual. The procedure reported here is significantly shortened, optimized to reduce side products, and avoids losses during sample handling. It can easily be adapted to any automated version of the sequencers. Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Isothiocyanates; Methods; Molecular Sequence Data; Muramidase; Pyridines; Ribosomal Proteins; Thiocyanates | 1991 |