ISOLATION OF TWO PANTOTHEINE‐CONTAINING ACIDIC PROTEINS FROM MONKEY BRAIN

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Abstract
The isolation of two acid‐soluble proteins from Macaca irus brain is reported. The proteins contained 34 and 35.6 per cent polar amino acids, respectively. One protein had a mol. wt. of approx. 37,100 and the other of 23,000 with subunits of 11,500. Each protein contained 4′‐phosphopantetheine, which was hydrolytically determined as taurine and β‐alanine and microbiologically as pantothenate. The smaller protein is found to be present in the supernatant following homogenization both in 0‐32 M‐sucrose and in 0‐32 M‐sucrose with 40 mm‐NaCl. The larger protein is also mainly present in the supernatant fluid. The function of these proteins is unknown, but the mol. wt. 23,000 species could be acetylated from glucose and acetate in mouse brain tissue slices and the acetyl groups could be isolated as the hydroxamate.