Key result
Human lung ACE purification reveals distinct N-terminal sequence from kidney enzyme with ~26% yield.
Why the study?
Purification and characterization of human lung angiotensin-converting enzyme were needed to understand its properties and sequence differences from other species and tissues.
Answers are grounded in this paper and cite their sources.
Provides purified human lung ACE for mechanistic studies; leaves open clinical translation to hypertension therapies.
Angiotensin-converting enzyme from the human lung was purified to apparent homogeneity, using high-performance liquid chromatography following trypsin treatment of the detergent-extract. A 1,750-fold purification was achieved with a 26% yield. The specific activity of the enzyme was 105 units per mg protein with the substrate hippuryl-L-histidyl-L-leucine (HHL) at 37 degrees C, and the Km value for HHL was 1.9 mM. The molecular weight was estimated to be 170,000 by sodium dodecyl sulfate gel electrophoresis, and the isoelectric point was about 4.8, by chromatofocusing. The N-terminal amino acid sequence was (NH2)-X-X-Pro-Gly-Leu-Glu-Pro-Gly-X-Phe-Ser-Ala-Arg-Glu-Ala-Gly-Ala. This is highly homologous to the corresponding sequences of the enzymes from bovine and rabbit lung and from pig, bovine, and mouse kidney, but significantly different from that of the human kidney enzyme.
No takes yet. Share an insight, caveat, or question.
Takeuchi et al. (1989) studied this question. High-performance liquid chromatography purification was evaluated on Enzyme purification yield and biochemical properties. Purification of human lung angiotensin-converting enzyme achieved a 1,750-fold purification with a 26% yield, revealing an N-terminal sequence distinct from the human kidney enzyme.
Synapse has enriched 10 related papers. Consider them for comparative context: