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Merck

G0535

Sigma-Aldrich

糖肽酶 A 来源于杏仁

buffered aqueous glycerol solution, ≥0.05 unit/mL

别名:

N-糖苷酶A, N-连接糖肽-(N-乙酰基-β-D-氨基葡萄糖)-L-天冬酰胺酰胺水解酶, 糖酰胺酶A

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About This Item

CAS号:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.32

共軛

(N-linked)

品質等級

形狀

buffered aqueous glycerol solution

濃度

≥0.05 unit/mL

儲存溫度

−20°C

一般說明

杏仁中发现的糖肽酶可分为 A、B 和 C 三组。糖肽酶 A 的最适 pH 值和等电点分别为 6.0 和 7.7。它偏爱长链糖肽。它还能够水解完整的糖蛋白,例如去唾液酸化的人转铁蛋白、卵清蛋白等。这些蛋白质在它们的 β-天冬氨酰-葡糖基胺键处切割具有去唾液酸碳水化合物部分的糖蛋白。

應用

来自杏仁的糖肽酶 A 用于去糖基化。它催化去除 N-连接的寡糖链并将 Asn 残基转化为 Asp。

生化/生理作用

水解 N4-(乙酰基-D-葡糖胺基)天冬酰胺,其中 N-乙酰基-D-葡糖胺残基可进一步糖基化,产生(取代的)N-乙酰基-β-D-葡糖胺基胺和含有天冬氨酸残基的肽。

單位定義

在 pH 5.0、37°C 条件下,1 个单位将每分钟水解1.0 μmole 卵清蛋白糖肽。

外觀

含 50 mM 柠檬酸盐-磷酸盐缓冲液(pH 5.0)和 BSA 的 50% 甘油溶液。

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

No data available

閃點(°C)

No data available


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Karen G Welinder et al.
The Journal of biological chemistry, 284(15), 9764-9769 (2009-02-13)
Proteome data of potato (Solanum tuberosum) tuber juice and of purified potato tuber vacuoles indicated that mature patatins may perhaps lack a C-terminal propeptide. We have confirmed this by complete mass spectrometric sequencing of a number of patatin variants as
Asparagine-linked oligosaccharides in human placenta and umbilical cord as demonstrated by almond glycopeptidase.
N Takahashi et al.
FEBS letters, 146(1), 139-142 (1982-09-06)
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Biochimica et biophysica acta, 657(2), 457-467 (1981-02-13)
The glycopeptidase preparation that has been isolated from almond emulsin and acts on beta-aspartylglycosylamine linkages in glycopeptides was separated into three active fractions by DEAE-cellulose column chromatography. The three discrete species of glycopeptidase (Groups A, B and C) have been
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Biochimica et biophysica acta, 954(1), 50-57 (1988-04-28)
The beta-subunit of dog kidney (Na+ + K+)-ATPase is a sialoglycoprotein and contains three potential N-glycosylation sites. In this study, the oligosaccharide chains of purified dog kidney beta-subunit were labeled with tritium by oxidation with sodium periodate or galactose oxidase
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Journal of biotechnology, 161(3), 336-348 (2012-07-21)
Glycosylation is one of the most common posttranslational modifications of proteins. It has important roles for protein structure, stability and functions. In vivo the glycostructures influence pharmacokinetics and immunogenecity. It is well known that significant differences in glycosylation and glycostructures

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N-Linked Glycan Strategies. Use of the endoglycosidic enzyme PNGase F (N-Glycosidase F) is the most effective method of removing virtually all N-linked oligosaccharides from glycoproteins.

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