Lysozyme (Muramidase)
(Synonyms: 溶菌酶; Muramidase) 目录号 : GC32682
溶菌酶（胞壁酶）是一种由动物产生的抗菌酶，是先天免疫系统的一部分。
Cas No.:9001-63-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Lysozyme is an antimicrobial enzyme produced by animals that forms part of the innate immune system.
[1]. Feingold DS, et al. Locus of the action of serum and the role of lysozyme in the serum bactericidal reaction. J Bacteriol. 1968 Dec;96(6):2118-26.
| Cas No. | 9001-63-2 | SDF | |
| 别名 | 溶菌酶; Muramidase | ||
| Canonical SMILES | Arg-Val-Val-Arg-Asp-Pro-Gln-Gly-Ile-Arg-Ala-Trp-Val-Ala-Trp-Arg-Asn-Arg | ||
| 分子式 | 分子量 | ||
| 溶解度 | Soluble in DMSO; H2O : 4.76 mg/mL (ultrasonic and adjust pH to 4 with 0.1 M HCL) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
[Lysozyme]
Nihon Rinsho 1995 May;53(5):1209-12.PMID:7602780doi
In the first section the assay methods of Lysozyme are reviewed. It is pointed out that there is no method using the hydrolysis of NAM- > beta-1, 4-glycoside bond- > NAG, So to clarify relation between methods will lead to discovery of new isozymes. In the second chapter serum or urinary Lysozyme levels are discussed in the states of diseases. The high levels are induced by cell proliferation which are producing Lysozyme. The type of cells and their nature may infer different lysozymes that has no clear evidences yet. In the third part Lysozyme is reviewed as protein and product of gene. In the final, enzyme kinetics are the subject of investigation, and further studies may by chance conduct us to find out new isozymes of Lysozyme in near future.
Lysozyme: a model protein for amyloid research
Adv Protein Chem Struct Biol 2011;84:63-111.PMID:21846563DOI:10.1016/B978-0-12-386483-3.00003-3.
Ever since Lysozyme was discovered by Fleming in 1922, this protein has emerged as a model for investigations on protein structure and function. Over the years, several high-resolution structures have yielded a wealth of structural data on this protein. Extensive studies on folding of Lysozyme have shown how different regions of this protein dynamically interact with one another. Data is also available from numerous biotechnological studies wherein Lysozyme has been employed as a model protein for recovering active recombinant protein from inclusion bodies using small molecules like l-arginine. A variety of conditions have been developed in vitro to induce fibrillation in hen Lysozyme. They include (a) acidic pH at elevated temperature, (b) concentrated solutions of ethanol, (c) moderate concentrations of guanidinium hydrochloride at moderate temperature, and (d) alkaline pH at room temperature. This review aims to bring together similarities and differences in aggregation mechanisms, morphology of aggregates, and related issues that arise using the different conditions mentioned above to improve our understanding. The alkaline pH condition (pH 12.2), discovered and studied extensively in our lab, shall receive special attention. More than a decade ago, it was revealed that mutations in human Lysozyme can cause accumulation of large quantities of amyloid in liver, kidney, and other regions of gastrointestinal tract. Understanding the mechanism of Lysozyme aggregation will probably have therapeutic implications for the treatment of systemic nonneuropathic amyloidosis. Numerous studies have begun to focus attention on inhibition of Lysozyme aggregation using antibody or small molecules. The enzymatic activity of Lysozyme presents a convenient handle to quantify the native population of Lysozyme in a sample where aggregation has been inhibited. The rich information available on Lysozyme coupled with the multiple conditions that have been successful in inducing/inhibiting its aggregation in vitro makes Lysozyme an ideal model protein to investigate amyloidogenesis.
What is new in Lysozyme research and its application in food industry? A review
Food Chem 2019 Feb 15;274:698-709.PMID:30372997DOI:10.1016/j.foodchem.2018.09.017.
Lysozyme, an important bacteriostatic protein, is widely distributed in nature. It is generally believed that the high efficiency of Lysozyme in inhibiting gram-positive bacteria is caused by its ability to cleave the β-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine. In recent years, there has been growing interest in modifying Lysozyme via physical or chemical interactions in order to improve its sensitivity against gram-negative bacterial strains. This review addresses some significant techniques, including sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), infrared (IR) spectra, fluorescence spectroscopy, nuclear magnetic resonance (NMR), UV-vis spectroscopy, circular dichroism (CD) spectra and differential scanning calorimetry (DSC), which can be used to characterize lysozymes and methods that modify lysozymes with carbohydrates to enhance their various physicochemical characteristics. The applications of biomaterials based on lysozymes in different food matrices are also discussed.
Engineering of Lysozyme
EXS 1996;75:163-81.PMID:8765300DOI:10.1007/978-3-0348-9225-4_10.
As the most extensively investigated model protein, the protein engineering of Lysozyme is described. By utilizing modifications made possible by chemical or gene engineering methods, we can get a better understanding of protein behaviour and we can also improve their properties. The results of the protein engineering of Lysozyme are described, which give some ideas for a better understanding of the physiological function of proteins, their stabilization, and how to engineer a novel protein.
[Lysozyme--occurrence in nature, biological properties and possible applications]
Postepy Hig Med Dosw (Online) 2014 Dec 21;68:1501-15.PMID:25531714DOI:10.5604/17322693.1133100.
Lysozyme (LZ, Muramidase, N-acetylmuramylhydrolase) is a protein occuring in animals, plants, bacteria and viruses. It can be found e.g. in granules of neutrophils, macrophages and in serum, saliva, milk, honey and hen egg white. The enzyme hydrolyzes the β-1,4 glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) of cell wall peptidoglycan (PG) in Gram-positive and Gram-negative bacteria. In the animal kingdom, three Muramidase types have been identified: the c-type (chicken type), the g-type (goose-type) and the i-type (invertebrates). The c-type LZ from hen egg white is a model for the study of protein structure and function. Muramidase shows bactericidal activity mainly against Gram-positive bacteria. Cytolytic activity against cells of Gram-negative bacteria has not been proved. Bacterial cells have developed defense mechanisms that allow them to avoid the action of LZ. They are based e.g. on the production of enzyme inhibitors or modification of the PG. LZ is one of the most studied enzymes and yet not all aspects characterizing this protein are fully understood. One of the most important unresolved issues concerning the biological function of LZ is the role of Muramidase in the bactericidal action of serum against Gram-negative bacteria. In order to clarify the function of LZ, the enzyme is e.g. removed from the serum by adsorption onto bentonite (montmorillonite, MMT). By using X-ray diffraction techniques it has been shown that MMT after contact with the serum is delaminated. The problems associated with folding of Muramidase and LZ participation in the development of amyloidoses also await explanation.