Purification of the angiotensin I-converting enzyme of the lung

Pig kidney angiotensin converting enzyme. Purification and characterization of amphipathic and hydrophilic forms of the enzyme establishes C-terminal anchorage to the plasma membrane

“…A fourth form of pig kidney ACE was solubilized merely by incubating the membranes at 37°C; after affinity purification this was termed the e-form. An endogenous mechanism for releasing ACE has been previously observed on homogenization of lung tissue (Igic et al, 1972;Nakajima et al, 1973;Patchett & Cordes, 1985). The e-form of pig kidney ACE had properties identical with those of the d-and t-forms with respect to its Mr on SDS/polyacrylamide-gel electrophoresis (Figs.…”

A Modern Understanding of the Traditional and Nontraditional Biological Functions of Angiotensin-Converting Enzyme

“…This served as a major impediment to detailed characterization, and was finally solved when model tripeptide substrates such as hippuryl-His-Leu, hippurylGly-Gly, and benzyloxycarbonyl (Z)-Phe-His-Leu were developed (Cushman and Cheung, 1969;Piquilloud et al, 1970;Yang et al, 1970). These and similar assays were used to purify ACE first from pig lung (Dorer et al, 1972;Nakajima et al, 1973). By 1980, ACE had been purified from the lung of pig, rabbit, dog, and cow, and from the sera of rabbit and humans (Soffer, 1981).…”

Biological and biochemical properties of angiotensin-converting enzyme

“…Molecular weights of electrophoretically homogeneous converting enzymes from other species have been estimated using Sephadex G-200 [18,[28][29][30] or gel electrophoresis at a single acrylamide concentration [17,29]. The reported figures were all much greater than ours; however, these techniques often give spuriously high values with glycoproteins.…”

“…The reported figures were all much greater than ours; however, these techniques often give spuriously high values with glycoproteins. They have also recently found (personal communication) that the rat enzyme and samples of two reportedly pure hog lung preparations [28,29] stained positively for carbohydrate and migrated identically to the rabbit lung enzyme during gel electrophoresis under native or reducing, denaturing conditions. They have also recently found (personal communication) that the rat enzyme and samples of two reportedly pure hog lung preparations [28,29] stained positively for carbohydrate and migrated identically to the rabbit lung enzyme during gel electrophoresis under native or reducing, denaturing conditions.…”