The specificity of the renin-angiotensinogen reaction through the phylogenetic scale. 1973

H L Nolly, and J C Fasciolo

UI MeSH Term Description Entries
D008322 Mammals Warm-blooded vertebrate animals belonging to the class Mammalia, including all that possess hair and suckle their young. Mammalia,Mammal
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011498 Protein Precursors Precursors, Protein
D012083 Renin A highly specific (Leu-Leu) endopeptidase that generates ANGIOTENSIN I from its precursor ANGIOTENSINOGEN, leading to a cascade of reactions which elevate BLOOD PRESSURE and increase sodium retention by the kidney in the RENIN-ANGIOTENSIN SYSTEM. The enzyme was formerly listed as EC 3.4.99.19. Angiotensin-Forming Enzyme,Angiotensinogenase,Big Renin,Cryorenin,Inactive Renin,Pre-Prorenin,Preprorenin,Prorenin,Angiotensin Forming Enzyme,Pre Prorenin,Renin, Big,Renin, Inactive
D012104 Reptiles Cold-blooded, air-breathing VERTEBRATES belonging to the class Reptilia, usually covered with external scales or bony plates. Reptilia,Reptile
D005075 Biological Evolution The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics. Evolution, Biological
D005399 Fishes A group of cold-blooded, aquatic vertebrates having gills, fins, a cartilaginous or bony endoskeleton, and elongated bodies covered with scales.
D000663 Amphibians VERTEBRATES belonging to the class amphibia such as frogs, toads, newts and salamanders that live in a semiaquatic environment. Amphibia,Amphibian
D000804 Angiotensin II An octapeptide that is a potent but labile vasoconstrictor. It is produced from angiotensin I after the removal of two amino acids at the C-terminal by ANGIOTENSIN CONVERTING ENZYME. The amino acid in position 5 varies in different species. To block VASOCONSTRICTION and HYPERTENSION effect of angiotensin II, patients are often treated with ACE INHIBITORS or with ANGIOTENSIN II TYPE 1 RECEPTOR BLOCKERS. Angiotensin II, Ile(5)-,Angiotensin II, Val(5)-,5-L-Isoleucine Angiotensin II,ANG-(1-8)Octapeptide,Angiotensin II, Isoleucine(5)-,Angiotensin II, Valine(5)-,Angiotensin-(1-8) Octapeptide,Isoleucine(5)-Angiotensin,Isoleucyl(5)-Angiotensin II,Valyl(5)-Angiotensin II,5 L Isoleucine Angiotensin II,Angiotensin II, 5-L-Isoleucine

Related Publications

H L Nolly, and J C Fasciolo
August 1965, Nature,
H L Nolly, and J C Fasciolo
February 1970, Bollettino della Societa italiana di biologia sperimentale,
H L Nolly, and J C Fasciolo
July 1966, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
H L Nolly, and J C Fasciolo
February 1972, Science (New York, N.Y.),
H L Nolly, and J C Fasciolo
December 1973, Biochemical pharmacology,
H L Nolly, and J C Fasciolo
February 2019, The Journal of biological chemistry,
H L Nolly, and J C Fasciolo
February 1970, Bollettino della Societa italiana di biologia sperimentale,
H L Nolly, and J C Fasciolo
January 1979, Clinica chimica acta; international journal of clinical chemistry,
H L Nolly, and J C Fasciolo
January 1974, Acta physiologica latino americana,
H L Nolly, and J C Fasciolo
June 1965, The American journal of physiology,
Copied contents to your clipboard!