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RESEARCH PRODUCT
Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP).
Valdis BerzinsAinars SkangalsViesturs BaumanisIlona MandrikaInta Jansonesubject
PhysiologyMuscle RelaxationRecombinant Fusion ProteinsRenal functionEnzyme-Linked Immunosorbent AssayIn Vitro TechniquesBiochemistryMuscle Smooth Vascularlaw.inventionCellular and Molecular NeuroscienceEndocrinologyCapsidAtrial natriuretic peptideIn vivolawEscherichia coliAnimalsAntihypertensive AgentsAortaChromatography High Pressure LiquidbiologyMolecular massChemistryMetalloendopeptidasesFusion proteinNPR2DiuresisRatsBiochemistryPolyclonal antibodiescardiovascular systembiology.proteinRecombinant DNACapsid ProteinsRabbitshormones hormone substitutes and hormone antagonistsAtrial Natriuretic Factorcirculatory and respiratory physiologyGlomerular Filtration Ratedescription
Abstract Baumanis, V., I. Jansone, A. Skangals, I. Mandrika and V. Berzins. Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP). Peptides 18(8) 1229–1235, 1997.—Recombinant atrial natriuretic peptide (rANP) was expressed in and isolated from E. coli. rANP was purified using HPLC. Amino acid analysis, partial sequencing, and molecular mass were determined. Fused protein was used to rise polyclonal antibodies and to develop of immunoenzymatic assays of rANP and CP/ANP. Experiments were designed to study rANP effects on isolated rabbit aortic strips and to examine hypotensive, diuretic, and natriuretic activity, as well as renal creatinine clearance, in an in vivo rat model. Identity of recombinant and commercial ANP has been confirmed. Physiological activity of CP/ANP has allowed the investigators to predict the conformation of CP/ANP, pro-ANP processing, and the method by which fusion protein interacts with ANP receptors.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-01-01 | Peptides |