STUDIES OF WATER SOLUBLE LIPOPROTEINS IN RAT BRAIN*

Authors

  • N. Herschkowitz,

    1. Departments of Pediatrics and Genetics, Lt. Joseph P. Kennedy Jr. Laboratories for Molecular Medicine, Stanford University School of Medicine, Palo Alto, California
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  • G. M. Mckhann†,

    1. Departments of Pediatrics and Genetics, Lt. Joseph P. Kennedy Jr. Laboratories for Molecular Medicine, Stanford University School of Medicine, Palo Alto, California
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  • E. M. Shooter

    1. Departments of Pediatrics and Genetics, Lt. Joseph P. Kennedy Jr. Laboratories for Molecular Medicine, Stanford University School of Medicine, Palo Alto, California
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  • *

    These studies were supported by funds from the Lt. Joseph P. Kennedy Jr. Foundation, the John A. Hartford Foundation, research grants NB-05300 and NB-04270 from the National Institute of Neurological Diseases and Blindness, United States Public Health Service, and research grant HD-02147 and training grant HD-00049 from the National Institute of Child Health and Human Development, United States Public Health Service.

  • Acknowledgements—The authors are grateful for the skillful technical assistance of Miss Shakuntla Saxena. They wish also to acknowledge John McKnight who performed the immunological investigations.

Abstract

—The occurrencc of water soluble lipoprotein in the 105,000 g supernatant of rat brain homogenate has been demonstrated.

The lipoproteins of brain differed from those of the serum with respect to lipid composition, density and reaction to serum lipoprotein antibodies.

Acrylamide gel electrophoresis resolved the brain supernatant into four zones which stained with lipid dye. It was possible to demonstrate that these zones also contained protein by double staining of the gel for lipid and protein. Two of the zones differed in their mobility from serum lipoprotein.

Preparative acrylamide gel electrophoresis isolated protein fractions in supematant which contained both lipid and protein and permitted preliminary identification of the lipoprotein bands amongst all the protein bands resolved by acrylamide gel electrophoresis.

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