Brush Border Particulates of Renal Tissue

Particulates containing a large part of the alkaline phosphatase activity of renal tissue were separated from homogenates and from ribosomal preparations by zonal centrifugation. The particles had a high content of phospholipid and cholesterol that was not removed by treatment with 1 percent deoxych...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1968-11, Vol.162 (3857), p.1009-1011
Main Authors: Binkley, Francis, King, Neva, Milikin, Elizabeth, Wright, Reba K., C. H. O' Neal, Wundram, Ina Jane
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - pharmacology
Alkaline Phosphatase - metabolism
Amino acids
Animals
Carbon Isotopes
Centrifugation
Centrifugation, Zonal
Cholesterols
Composite particles
Enzymes
Glucose-6-Phosphatase - metabolism
Kidney Tubules - cytology
Kidney Tubules - enzymology
Leucine - metabolism
Membranes - enzymology
Microscopy, Electron
Microvilli
P branes
Particulate matter
Peptide Hydrolases - metabolism
Phosphatases
Puromycin - pharmacology
Pyrophosphatases - metabolism
Rats
Ribosomes - enzymology
Surface-Active Agents
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Summary:Particulates containing a large part of the alkaline phosphatase activity of renal tissue were separated from homogenates and from ribosomal preparations by zonal centrifugation. The particles had a high content of phospholipid and cholesterol that was not removed by treatment with 1 percent deoxycholate. Enzymatic activities concentrated with the particles were the alkaline phosphatase, a peptidase resistant to proteolysis, glucose-6-phosphatase, inorganic pyrophosphatase, and adenosine triphosphatase. The particles accumulated leucine with no stimulation from soluble factors and with inhibition by other amino acids; the accumulation was stimulated by adenosine triphosphate and was not inhibited by puromycin. The particles appear to be derived from the membranes of the brush borders of tubular cells.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.162.3857.1009