The Cytochemical Localization of Alkaline Phosphatase in Escherichia coli at the Electron-Microscope Level

Abstract

SHORT COMMIUNICATIONS 27c pronounced change in the ratio of the trans to the cw forms, with the concentration of the former always being several times greater than that of the latter. There was little evidence of double-bond migration under normal conditions. The conjugated linoleic acid and linolenic acid have retention volumes greater than those ofthe normal compounds and could be separated by gas-liquid chromatography (Daniels & Richmond, 1960). No conjugated linoleic acid and linolenic acid could be detected either during control periods or during periods in which oleic acid was infused. Conjugates accounted for 5-10% of the polyenoic acids during infusion of small amounts of nonconjugated linoleic acid and linolenic acid and 15-25% during infusion of larger amounts. The conjugated polyenoic acids are hydrogenated with difficulty (Garton, 1959) and would be expected to accumulate to a much greater extent than the non-conjugated acids. The above results offer no support for the hypothesis that the process of hydrogenation involves appreciable bond migration and accumulation of conjugated acids (Shorland et al. 1957; Kepler et al. 1965), but they are consistent with the hypothesis that elaidic acid, and not oleic acid, is an intermediate in the hydrogenation of the polyenoic acids in the rumen. We are grateful to Miss G. H. McG. Breckenridge for her assistance with the analyses.

Acid and alkaline phosphatases of Capnocytophaga species. I. Production and cytological localization of the enzymes

“…In Bacterionema and Actinomyces, A1P and (or) its synthesis was inhibited by 10 mM Na2HP04 (Franker et al 1978), while in E. coli the synthesis of an inducible A1P was repressed in the presence of 2.3 mM Pi in the growth media (Done et al 1965;Torriani 1960). Cheng et al (1970~) and Hou et al (1966) found that, in P. aeruginosa, there was a 500-fold decrease in A1P activity in the presence of 7 mM Pi.…”

“…The most extensively investigated periplasmic phosphatase has been Alp. In E. coli (Done et al 1965;Heppel 1967) and P. aeruginosa (Cheng et al 1970a(Cheng et al , 1970bCheng et al 1972), it is localized almost exclusively in the periplasm, being released in toto by mild cell disruption; in fact with few exceptions (Lindsay et al 1973;Work et al 1966), most of the periplasmic enzymes appear to be "free" in the cells periplasm. While the release of cell components from gram-negative bacteria into the surrounding milieu is known (Russell 1976), the kinetics of release of periplasmic enzymes during cell growth has not been extensively studied.…”

“…These enzymes include the ribonucleases (Heppel 1967), the sulfate-binding proteins (Pardee and Watanabe 1968), and the cell envelope p-lactamases (Smith and Wyatt 1974). The phosphatases, such as cyclic phosphodiesterase (Brockman and Heppel 1968), 5'-nucleotidase (Bhatti et al 1976), and nonspecific phosphatases (phosphomonoesterases, AcP and Alp (Cheng et al 1970a;Done et al 1965;Voelz and Ortigosa 1968)) have a periplasmic location. AcP has both a cell wall and periplasmic location in Rhizobium (Truchet and Coulomb 1973) and Myxococcus (Voelz and Ortigosa 1968).…”

Electron microscopy of adenosine triphosphatase in Escherichia coli cells

“…A number of experiments were carried out by either tetrazolium or tellurite techniques in bacterial dehydrogenase cytochemistry (16, 23,[26][27][28][29]. Only a few papers have been concerned with phosphatase location (3,13,30).…”

The Ultrastructural Localization of Alkaline Phosphatase Isoenzymes in Some Normal and Malignant Cells

“…Done [4] studied the cytochemical localization of alkaline phosphat ase in Escherichia coli and found a remarkably well-defined compartmentalization. These observations were confirmed by Malamy and Horecker [15].…”