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Merck

C3888

Sigma-Aldrich

Carboxypeptidase Y aus Backhefe (S. cerevisiae)

lyophilized powder, ≥50 units/mg protein

Synonym(e):

Peptidyl-L-aminosäure-Hydrolase, Serin-Carboxypeptidase

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About This Item

CAS-Nummer:
EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Qualität

Proteomics Grade

Qualitätsniveau

Form

lyophilized powder

Spezifische Aktivität

≥50 units/mg protein

Mol-Gew.

61 kDa

Zusammensetzung

Protein, ≥75% E1%/280

Versandbedingung

wet ice

Lagertemp.

−20°C

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Anwendung

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.

Biochem./physiol. Wirkung

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.

Verpackung

Packungsgrösse bezogen auf den Proteingehalt.

Einheitendefinition

1 U hydrolysiert 1.0 μmol N-CBZ-Phe-Ala zu N-CBZ-L-Phenylalanin und L-Alanin pro Minute bei pH 6.75 und 25°C, basierend auf EM/230 = 191.5.

Physikalische Form

Enthält Citrat-Puffer, pH ~5

Hinweis zur Analyse

amidase and esterase activities may be present

Piktogramme

Exclamation markHealth hazard

Signalwort

Danger

Gefahreneinstufungen

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Caroline A Magalhães et al.
Memorias do Instituto Oswaldo Cruz, 106(2), 146-152 (2011-05-04)
Typical and atypical enteropathogenic Escherichia coli (EPEC) are considered important bacterial causes of diarrhoea. Considering the repertoire of virulence genes, atypical EPEC (aEPEC) is a heterogeneous group, harbouring genes that are found in other diarrheagenic E. coli pathotypes, such as
H R Stennicke et al.
Biochemistry, 35(22), 7131-7141 (1996-06-04)
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
L Ballou et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(9), 3368-3372 (1990-05-01)
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
Johanna Rankenberg et al.
Experimental eye research, 210, 108704-108704 (2021-07-25)
Advanced glycation end products (AGEs) accumulate with age in human lens capsules. AGEs in lens capsules potentiate the transforming growth factor beta-2-mediated mesenchymal transition of lens epithelial cells, which suggests that they play a role in posterior capsule opacification after
Václava Bauerová et al.
Canadian journal of microbiology, 58(5), 678-681 (2012-04-17)
Vacuoles play an important role in the physiology of pathogenic Candida spp. However, information on Candida albicans vacuolar enzymes, their properties, and regulation is scarce. Expression of the genes APR1 and CPY1 encoding vacuolar aspartic protease and serine carboxypeptidase, respectively

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