Affiliation:
1. Institute of Dental Research, Departments of Oral Pathology and Oral Biology, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48104, USA
Abstract
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.
Cited by
3 articles.
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