Comparative biochemistry of renins and angiotensins in the vertebrates.

Comparative biochemistry of renins and angiotensins was discussed. Renin extracted from hog kidney was different from that from mouse submaxillary glands in immunoreactivity and carbohydrate content. Rat kidney renin was also different from hog kidney renin in the amino acid composition. The presence of big and big-big renins was pointed out immunochemically. These big renins were considered to be precursors of kidney renin. Angiotensins in mammalian and nonmammalian species produced by renal or extrarenal renin have been differentiated by some biochemical and pharmacological criteria. Some of these angiotensins were analyzed sequentially. The replacements of amino acid residues at positions 1, 5, and/or 9 of angiotensin I have been demonstrated in nonmammalian species. Specific pressor activities have been determined using synthetic angiotensins by a 4 point assay in rat. Specific pressor activities of various angiotensins were obtained from the dose-blood pressure-response curves using a single angiotensin sample per assay rat.

[1]  T. Nakajima,et al.  Comparative studies on angiotensins. V. Structure of angiotensin formed by the kidney of Japanese goosefish and its identification by dansyl method. , 1978, Chemical & pharmaceutical bulletin.

[2]  T. Nakajima,et al.  Comparative studies on angiotensins. IV. Structure of snake (Elaphe climocophora) angiotensin. , 1977, Chemical & pharmaceutical bulletin.

[3]  T. Inagami,et al.  Purification of high molecular weight forms of renin from hog kidney. , 1977, Circulation research.

[4]  T. Inagami,et al.  Pure Renin. Isolation from hog kidney and characterization. , 1977, The Journal of biological chemistry.

[5]  S. Sakakibara,et al.  Specific pressor activity and stability of synthetic angiotensins. , 1977, Japanese journal of pharmacology.

[6]  R. Vergona,et al.  Fluorescamine as a terminating agent in solid phase peptide synthesis. , 2009, International journal of peptide and protein research.

[7]  H. Sokabe Phylogeny of the renal effects of angiotensin. , 1974, Kidney international.

[8]  H. Sokabe,et al.  Comparative studies of the juxtaglomerular apparatus. , 1974, International review of cytology.

[9]  J. Ménard,et al.  Pepstatin, an inhibitor for renin purification by affinity chromatography , 1973, FEBS letters.

[10]  T. Nakajima,et al.  Comparative studies on angiotensins. 3. Structure of fowl angiotensin and its identification by DNS-method. , 1973, Chemical & pharmaceutical bulletin.

[11]  J. Taylor,et al.  Isolation and characterization of renin-like enzymes from mouse submaxillary glands. , 1972, Biochemistry.

[12]  T. Nakajima,et al.  Comparative studies on angiotensins. II. Structure of rat angiotensin and its identification by DNS-method. , 1972, Chemical & pharmaceutical bulletin.

[13]  T. Nakajima,et al.  Examination of angiotensin-like substances from renal and extrarenal sources in mammalian and nonmammalian species. , 1971, General and comparative endocrinology.

[14]  K. Arakawa,et al.  Isolation and amino acid composition of human angiotensin I. , 1967, The Biochemical journal.

[15]  B. Riniker RECENT WORK ON THE CHEMISTRY AND BIOCHEMISTRY OF ANGIOTENSIN II. , 1964, Metabolism: clinical and experimental.

[16]  J. de Champlain,et al.  NEW PROCEDURES FOR MEASUREMENT OF HUMAN PLASMA ANGIOTENSIN AND RENIN ACTIVITY LEVELS. , 1964, Canadian Medical Association journal.

[17]  I. Page,et al.  Synthesis and Properties of Angiotonin , 1958, Circulation.

[18]  D. F. Elliott,et al.  Amino-acid sequence in a hypertensin. , 1957, Nature.

[19]  K. R. Woods,et al.  THE AMINO ACID SEQUENCE OF HYPERTENSIN II , 1956, The Journal of experimental medicine.