Search by BoMiProt ID - Bomi158


Primary Information

BoMiProt ID Bomi158
Protein Name Lysozyme C, milk isozyme
Organism Bos taurus
Uniprot IdQ6B411
Milk FractionWhey
Ref Sequence Id NP_001071297.1
Amino Acid Lenth 148
Molecular Weight 16783
Fasta Sequence https://www.uniprot.org/uniprot/Q6B411.fasta
Gene Name LYZ1
Gene Id 281287
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells tears, saliva, milk, mucus
Protein Function antimicrobial activity; catalyses the hydrolysis of glycosidic bonds of mucopolysaccharides in bacterial cell walls; immune-regulatory activities, inactivation of certain viruses; antiinflammatory; antitumour
Biochemical Properties Optimum pH of 7.9 in 0.067 M phosphate buffer; require salts for activity; sodium citrate was the most potent activator of the enzyme activity; sedimentation coefficient 2S; isoelectric point to be around pH 9.5; more stable in a.IS M KC1-o.o2 :M sodium acetate buffer (pH 5.4) than in aqueous solution; labile at alkaline pH; Any treatment which "increases the acid character of the molecule decreases the enzyme's potency, and the treatments which increase its basic character increase its activity;
Significance in milk role of fighting infections in breastfeeding infants; natural antimicrobial agent;
Bibliography 1. Ozturkoglu-Budak, S. (2018). Effect of different treatments on the stability of lysozyme, lactoferrin and β-lactoglobulin in donkey’s milk. International Journal of Dairy Technology, 71(1), 36–45. https://doi.org/10.1111/1471-0307.12380.
2. Chandan, R. C., Parry, R. M., & Shahani, K. M. (1965). Purification and some properties of bovine milk lysozyme. Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 110(2), 389–398. https://doi.org/10.1016/S0926-6593(65)80046-7.