Comparison of casein of cynomolgus monkey (Macaca fascicularis) with human casein

Abstract

• 1. Casein of cynomolgus monkey was compared with those from human and bovine milk. Cynomolgus monkey casein showed similar electrophoretical patterns to those of human casein on Disc- and SDS-electrophoresis. It consisted of β- and κ-casein-like components. The component corresponding to bovine $\text{α}{}_{\mathrm{<mtext>s</mtext><mtext>1</mtext>}}\text{-}\text{casein}$ was not detected.

• 2. The β-casein-like fraction of cynomolgus monkey showed 9 bands on Disc-PAGE. These were suggested to be the same protein binding different levels of phosphorus by dephosphorylation experiment using an acid phosphatase.

• 3. The κ-casein-like component of cynomolgus monkey was highly glycosilated (about 50% carbohydrate) similarly as human κ-casein and the constituent carbohydrates were same as those detected in human κ-casein (galactose, fucose, $\text{N-}\text{acetylgalactosamine}$, $\text{N-}\text{acetylglucosamine}$, and sialic acid).

• 4. Amino acid composition of cynomolgus monkey κ-casein bore a resemblance to those of both human and bovine κ-caseins. Amino acid composition of cynomolgus monkey β-casein was also similar to those of human and bovine β-caseins.