C3888
Carboxypeptidase Y from baker′s yeast (S. cerevisiae)
lyophilized powder, ≥50 units/mg protein
Sinonimo/i:
Peptidyl-L-amino acid Hydrolase, Serine Carboxypeptidase
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About This Item
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54
Prodotti consigliati
Grado
Proteomics Grade
Livello qualitativo
Forma fisica
lyophilized powder
Attività specifica
≥50 units/mg protein
PM
61 kDa
Composizione
Protein, ≥75% E1%/280
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
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Categorie correlate
Applicazioni
Carboxypeptidase Y has a broad specificity and is stable in urea. Hence, this enzyme is not like other carboxypeptidases and can be used for sequence analysis. Due to its amidase action, this enzyme might be applied to the sequence analysis of peptides having amidated COOH-terminal groups such as oxytocin and vasopressin.
Azioni biochim/fisiol
The glycoprotein has a molecular weight of about 61,000, has a nitrogen content of 12.74%. It is a single polypeptide chain of 442 residues with 16 residues of glucosamine in the carbohydrate moiety. Lysine is at the NH2 terminus and -Asp-Ser-Thr-Leu is the COOH-terminal sequence. The principal action of the enzyme is to remove COOH-terminal residues from polypeptide chains. It is used as a vacuolar marker enzyme for studies on protein transport and localization.
Confezionamento
Package size based on protein content
Definizione di unità
One unit will hydrolyze 1.0 μmole of N-CBZ-Phe-Ala to N-CBZ-L-phenylalanine and L-alanine per min at pH 6.75 at 25°C, based on EM/230 = 191.5.
Stato fisico
Lyophilized powder containing citric acid.
Risultati analitici
amidase and esterase activities may be present
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organi bersaglio
Respiratory system
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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The activity of serine carboxypeptidases is dependent on a catalytic triad, an oxyanion hole, and a binding site equivalent to those found in the serine endopeptidases. The action of carboxypeptidase Y on substrates containing amino acids, alcohols, and amines as
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The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn
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