Regeneration of amino acids from thiazolinones formed in the Edman degradation

Méndez, Enrique; Lai, Chun‐Yen

doi:10.1016/0003-2697(75)90677-6

Cited by 395 publications

(82 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Identification of the PTH-amino acids was made by HPLC as described by SVENDSEN et al (20). Additional information was obtained by thin layer chromatography on polyamide sheets according to KULaE (14) or by back hydrolyses to the free amino acids as described by MENDEZ and LAa (18), For peptides shorter than 50 residues Polybrene was added in order to minimize extractive losses of peptide material (12). Column dimension 2.6 x 100 era.…”

Section: 212 Amino Acid Sequencingmentioning

confidence: 99%

Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages

Svendsen

Martin

Viswanatha

et al. 1982

Carlsberg Res. Commun.

View full text Add to dashboard Cite

Keywords: Carboxypeptidase Y, a m i n o acid sequence, yeast Carboxypeptidase Y (E.C.3.4.12. I) with the lysine side-chains blocked by citraconylation has been digested with trypsin and the resulting peptides purified by gel filtration followed by ion-exchange chromatography on DE 52 cellulose. Eight of the expected ten peptides have been completely or partially sequenced in a liquid phase automatic sequencer. The remaimng two peptides were sequenced as part of a CNBr peptide (see preceeding paper). Selected peptides obtained from enzymatic cleavages with A. mellea protease, chymotrypsin, post-proline cleaving enzyme, S. aureus V8 protease, and subtilisin have upon sequencing provided overlaps which have made the reconstruction of 96 % of the complete sequence possible together with a tentative assignment of the carbohydrate attachment sites. No homology with sequences of known proteases has been observed.

show abstract

Section: 212 Amino Acid Sequencingmentioning

confidence: 99%

Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages

Svendsen

Martin

Viswanatha

et al. 1982

Carlsberg Res. Commun.

View full text Add to dashboard Cite

show abstract

“…Conversion to the PTH-amino acids was performed according to a published procedure (11), and the PTH-amino acids were identified by a combination of at least two of the following methods: a) high performance liquid chromatography (24), b) thin layer chromatography (21), c) back-hydrolysis to free amino acid (22), d) identification of histidine with Pauly's reagent (11) and of arginine with phenanthroquinone (16).…”

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

“…Back-hydrolysis to the parent amino acid was done at 150 ~ for four hours using 5.7 M-HC1 containing 0.1% SnC12 (22).…”

Section: Amino Acid Sequence Determinationmentioning

confidence: 99%

The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

Johansen

Overballe-Petersen

Martin

et al. 1979

Carlsberg Res. Commun.

View full text Add to dashboard Cite

The amino acid sequence of the copper,zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55 96 identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the ye,~st enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor. Superoxide dismutases (SOD) are a group of metalloenzymes, whose function is to scavenge the superoxide radical anion 02 (12) by catalyzing its dismutation to hydrogen peroxide and dioxygen:

show abstract

“…The amino acid sequence of smaller peptides was determined by a manual micro Edman technique [20] without dansylation. The thiazolinone or PTH derivatives were hydrolysed with 6 N HCI in the presence or absence of 0.1% SnCI2 [21] at 130°C for 20 h, and the amino acids formed were analysed with the Durrum analyzer. The identification of PTH derivatives was made by thin-layer chromatography on silica gel plates [22,23].…”

Section: Nrcc Publication No 16162mentioning

confidence: 99%

Primary structure of protein S19 from the small ribosomal subunit of Escherichia coli

1978

View full text Add to dashboard Cite

Regeneration of amino acids from thiazolinones formed in the Edman degradation

Cited by 395 publications

References 9 publications

Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages

Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages

The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

Primary structure of protein S19 from the small ribosomal subunit of Escherichia coli

Contact Info

Product

Resources

About