Lactosyl phosphate

The 1-phosphates of a- and /3-lactose have been synthesized by interacting silver diphenyl phosphate with hepta-O-acetyl-a-lactosyl bromide, with the elimination of silver bromide, followed by hydrogenolysis of the phenyl groups and fractional recrystallization of the barium salts. /3-Lactosyl phosphate is more readily hydrolyzed than the a anomcr in N hydrochloric acid at 37° (64% and 26% hydrolysis, respectively, after 80 minutes). 

Fig. 2.—Elution Patterns for Samples of Rabbit Antisera from Lactosyl-agarose. [Initial elution with 0.02 M phosphate buffer, pH 7.2, in saline subsequent elution with 0.5 M D-galactose (first arrow), and with 0.5 M lactose (second arrow). Preimmune serum (A), anti-S. faecalis serum (B), anti-Gal-BSA serum (C), and anti-Lac-BSA serum (D) (see Ref. 143).]...

Glycosynthase activity for tetrasaccharide synthesis from a-lactosyl fluoride and p-nitrophenyl /3-cellobioside (PNPC) was measured for the Humicola insolens Cel7B variants in sodium phosphate buffer, pH 7.0, at room temperature. Specific activities were determined by measuring the fluoride ion release rate by a fluoride ion selective electrode. The protein purification yields are the yield of purified protein as determined by western analysis from total cell culture. 

Both the a- and jS-forms of lactose 1-phosphate have been prepared (230), The a-lactose 1-phosphate was synthesized by phosphorylating hepta-0-acetyl-a-lactosyl bromide with silver diphenyl phosphate. For the preparation of the jS-form of this ester monosilver phosphate was used as a phosphorylating agent 192),... 

The adenosine-3 -phosphate-5 -phosphosulfate (PAPS) generating system could be located in the 105,000 g supernatant of rat brain, whereas the Gal-Cer sulfotransferase remained particle bound. Substrate may be Gal-Cer or lactosyl ceramide. Sulfatides of kidney show a higher metabolic turnover than those in brain. Water-soluble sulfatide, discovered in the 105,000 g supernatant of a brain homogenate, was found to be complexed to certain specific proteins (Hersch-kowitz et al., 1968). It was postulated that this might represent a transport form from the site of biosynthesis to the myelin. 

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