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Activity of acid phosphatase and beta-glucuronidase was shown in bovine preodontoblasts and preameloblasts prior to the onset of secretion. In the preameloblasts the rather weak reaction consisted of small discrete granules dispersed in the cytoplasm apical, lateral, and proximal to the nucleus. After initiation of enamel formation, a change in localization(More)
Alkaline phosphatase (AP) from partly mineralized bovine enamel was studied. The enzyme resembles alkaline phosphatases in other calcifying tissues. The Km was 0.46 mM; the phosphatase was strongly inhibited by 1 mM Levamisol or EDTA and it showed the same sensitivity towards heating as bone alkaline phosphatase. The inactivation caused by phosphate ions(More)
ATP and 5-Br-4-Cl-indoxyl phosphate were used as substrates for spectrophotometric measurement of phosphatase activity in partly mineralized bovine enamel. MgCl2, CaCl2, NaCl, and KCl were used as moderators of the enzyme activities. It is concluded that at least two phosphatases, active at alkaline pH, are present in the immature enamel matrix.
Antiserum was raised against an acetic acid extract of partly mineralized bovine enamel. By use of immunoblotting it was shown that rabbit antibodies react with both high and low molecular weight proteins. Most but not all of the enamel proteins isolated by different extraction solutions were antigenic identical. The blotting time was found to be important(More)
Enamel proteins from fully mineralized human molars and from bovine tooth germs were separated by electrophoresis. The gels were stained for detection of glycoproteins, lipoproteins, and phosphoproteins. Glycoproteins were shown by periodic acid-Schiff staining and lectin blotting. In mature human enamel a number of high molecular weight proteins could be(More)
Alkaline phosphatase (AP) was prepared from partly mineralized bovine enamel by extraction in phosphate buffer, centrifugation and various chromatographic techniques. Chromatofocusing showed that the enamel enzyme possessed five isoelectric points at the acid pH level ranging from pH 5.7 to pH 4.4. Three enzyme peaks were eluted using low pressure(More)