Biochemical and morphological studies of rat submandibular gland: II. Partial purification of proteins from granule-rich fraction.
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.
D000468:Alkalies; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003594:Cytoplasmic Granules / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004950:Esterases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D004952:Esters; D005779:Immunodiffusion; D008297:Male; D010447:Peptide Hydrolases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology; D013363:Submandibular Gland / Q000201:enzymology* / Q000648:ultrastructure
D000468:Alkalies; D004952:Esters; D004950:Esterases; D010447:Peptide Hydrolases