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J Dent Res 54(5): 948-959, 1975
© 1975 International and American Associations for Dental Research
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Biochemical and Morphological Studies of Rat Submandibular Gland: II. Partial Purification of Proteins from Granule-Rich Fraction

S. G. CHAKRABARTI 1, C. T. HANKS 1, and S. P. JOHNSON 1

1 Institute of Dental Research, Departments of Oral Pathology and Oral Biology, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48104, USA

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.

Submitted on October 7, 1974
Accepted on March 4, 1975






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