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Merck
CN

62970

Lysozyme 来源于鸡蛋白

dialyzed, lyophilized, powder, ~100000 U/mg

别名:

粘肽N-乙酰胞壁质水解酶, 胞壁质酶

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
Specific activity:
~100000 U/mg
Biological source:
chicken egg white
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产品名称

Lysozyme 来源于鸡蛋白, dialyzed, lyophilized, powder, ~100000 U/mg

biological source

chicken egg white

form

powder

quality

dialyzed
lyophilized

specific activity

~100000 U/mg

mol wt

single-chain 14.3 kDa
Mr ~14600

technique(s)

cell based assay: suitable

suitability

suitable for cell lysis

UniProt accession no.

application(s)

cell analysis

storage temp.

2-8°C

Quality Level

Gene Information

chicken ... LYZ(396218)

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Application

来自鸡蛋清的溶菌酶已被用于:
  • 作为小角度中子散射实验 和红外吸收光谱的标准品
  • 在蛋白质结晶实验中,作为细胞裂解缓冲液的组分

酶可分解细菌的细胞壁;用于制备原生质体。

Biochem/physiol Actions

溶菌酶可水解肽聚糖中N-乙酰胞壁酸与N-乙酰-D-氨基葡萄糖残基之间以及壳糊精中N-乙酰-D-氨基葡萄糖残基之间的β(1→4)连接。 革兰氏阳性细胞对这种水解非常敏感,因为它们的细胞壁中的肽聚糖比例很高。革兰氏阴性菌就对这种水解没那么敏感,因为它们有外膜并且肽聚糖的比例较低。然而,这些细胞可能在细胞外膜中螯合金属离子的EDTA存在的情况下水解。

该酶在广泛的pH范围(6.0至9.0)内具有活性。pH值为6.2时,可在更广的离子强度范围(0.02至0.100 M)观察到最大活性,而pH值为9.2时为0.01至0.06 M。
溶菌酶可水解肽聚糖中N-乙酰胞壁酸与N-乙酰-D-氨基葡萄糖残基之间以及壳糊精中N-乙酰-D-氨基葡萄糖残基之间的β(1→4)连接。革兰氏阳性细胞对这种水解非常敏感,因为它们的细胞壁中的肽聚糖比例很高。

Other Notes

1 U对应于在pH7.0和25°C下,将酶在450nm处的吸光度降低0.001(每分钟0.001)所需的酶量[藤黄微球菌(Micrococcus luteus),ATCC 4698,作为底物]
适用于细菌细胞壁、粘多糖、粘多肽或几丁质的水解;可降解乳酸乳球菌乳脂亚种H2细胞壁;综述

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

动植物源性产品
低风险生物材料
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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T Coolbear et al.
Applied and environmental microbiology, 58(10), 3263-3270 (1992-10-01)
The cell wall-associated proteinase from Lactococcus lactis subsp. cremoris H2 (isolate number 4409) was released from the cells by treatment with lysozyme, even in the presence of 50 mM calcium chloride. Cell lysis during lysozyme treatment was minimal. The proteinase
R.W. Franck
Bioorganic Chemistry, 20, 77-77 (1992)
Infrared absorbance spectroscopy of aqueous proteins: Comparison of transmission and ATR data collection and analysis for secondary structure fitting
Corujo MP, et al.
Chirality, 30(8), 957-965 (2018)
L. Stevens
Comp. Biochem. Physiol., B: Comp. Biochem., 100, 1-1 (1991)
Structures and interactions among lysozyme proteins below the isoelectric point in presence of divalent ions
Pandit S, et al.
Chemical Physics Letters, 711, 8-14 (2018)

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