Biochemical and Morphological Studies of Rat Submandibular Gland: II. Partial Purification of Proteins from Granule-Rich Fraction.

Autor: CHAKRABARTI, S. G., HANKS, C. T., JOHNSON, S. P.
Předmět:
Zdroj: Journal of Dental Research; Sep1975, Vol. 54 Issue 5, p948-959, 12p, 2 Black and White Photographs, 3 Charts, 6 Graphs
Abstrakt: Soluble proteins derived from a centrifuged and filtered granule-rich fraction of homogenized rat submandibular gland were analyzed by gel filtration, ion-exchange chromatography, and polyacrylamide gel electrophoresis. Both the granule-rich fraction and final supernatant fraction contained alkaline esterase activity. The major protein component, derived from granules of the convoluted tubules, was further resolved into a series of peptides ranging in molecular weight from 9,000 to 55,000 daltons. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index