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bovine colustrum

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https://www.readbyqxmd.com/read/27854033/comparative-analysis-of-the-antiviral-activity-of-camel-bovine-and-human-lactoperoxidases-against-herpes-simplex-virus-type-1
#1
Esmail M El-Fakharany, Vladimir N Uversky, Elrashdy M Redwan
Lactoperoxidase is a milk hemoprotein that acts as a non-immunoglobulin protective protein and shows strong antimicrobial activity. Bovine milk contains about 15 and 7 times higher levels of lactoperoxidase than human colustrum and camel milk, respectively. Human, bovine, and camel lactoperoxidases (hLPO, bLPO, and cLPO, respectively) were purified as homogeneous samples with specific activities of 4.2, 61.3, and 8.7 u/mg, respectively. The optimal working pH was 7.5 (hLPO and bLPO) and 6.5 (cLPO), whereas the optimal working temperature for these proteins was 40 °C...
November 16, 2016: Applied Biochemistry and Biotechnology
https://www.readbyqxmd.com/read/5776530/sialidase-like-enzymes-produced-by-group-a-b-c-g-and-l-streptococci-and-by-streptococcus-sanguis
#2
S Hayano, A Tanaka
A group of enzymes were prepared from the culture fluids of streptococci belonging to groups A, B, C, G, and L, and from a strain of Streptococcus sanguis. These streptococcal enzymes (designated St-sialidases) released a substance shown to belong to the sialic acid group from the specific substrate BSM-St, a sialomucoid prepared from bovine submaxillary gland. They were inactive on N-acetylneuramin lactose prepared from bovine colustrum and on a sialomucoid prepared from bovine submaxillary mucin, whereas these substances are susceptible to sialidases produced by group K streptococci and by Vibrio cholerae...
March 1969: Journal of Bacteriology
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