Nothing Special   »   [go: up one dir, main page]

Poulsen et al., 1975 - Google Patents

Purification of hog renin by affinity chromatography using the synthetic competitive inhibitor [D-Leu6] octapeptide

Poulsen et al., 1975

Document ID
164227261760097583
Author
Poulsen K
Burton J
Haber E
Publication year
Publication venue
Biochimica et Biophysica Acta (BBA)-Protein Structure

External Links

Snippet

The renin substrate analog His-Pro-Phe-His-Leu-d-Leu-Val-Tyr ([d-Leu 6]-octapeptide) acts as a potent inhibitor of renin because of the d-amino acid substitution at the cleavage site. This inhibitor was coupled to CNBr-activated Sepharose 4B to yield a support for affinity …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K1/00General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14Extraction; Separation; Purification
    • C07K1/16Extraction; Separation; Purification by chromatography
    • C07K1/22Affinity chromatography or related techniques based upon selective absorption processes
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors

Similar Documents

Publication Publication Date Title
Ryle et al. Parapepsins: two proteolytic enzymes associated with porcine pepsin
Noyer et al. Purification and characterization of undegraded human ceruloplasmin
Okubo et al. Purification and immunological determination of α2-macroglobulin in serum from injured rats
US6677440B1 (en) Process for the preparation in pure form of the protease activating blood clotting factor VII, its proenzyme or a mixture of both proteins by means of ion-exchange chromatography
Kato et al. Purification of synthetic ribonuclease S-peptide derivatives by specific complex formation on columns of ribonuclease S-protein bound to agarose
CA2315309A1 (en) Process for the preparation in pure form of the protease activating blood clotting factor vii, its proenzyme or a mixture of both proteins by means of affinity chromatography
Bond et al. Isolation of bovine angiogenin using a placental ribonuclease inhibitor binding assay
Poulsen et al. Purification of hog renin by affinity chromatography using the synthetic competitive inhibitor [D-Leu6] octapeptide
Yokosawa et al. Purification of human renin
Kanoun et al. New support for the large-scale purification of proteins
Boman Chromatography of serum and some other proteins on an anion-exchange resin
FI96211C (en) Process for Separate Purification and Separation of Single-Chain Tissue Plasminogen Activator (tPA) and Double-Chain TPA from a Mixture
McINTYRE et al. Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H. 77 (D-His-Pro-Phe-His-Leu-R-Leu-Val-Tyr)
Bazzone et al. Single-step isolation and resolution of pancreatic carboxypeptidases A and B
Jameson et al. Affinity chromatography of bovine trypsin. A rapid separation of bovine α-and β-trypsin
Johnson et al. Partial purification and chromatographic properties of inactive renin from human amniotic fluid
Kuehn et al. Proteinase inhibitors in rat serum. Purification and partial characterization of three functionally distinct trypsin inhibitors
Pacaud Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase
JPH0224839B2 (en)
Banerjee et al. A convenient procedure for purification of thymidylate synthase from L1210 cells
Habal et al. Kininogens of human plasma
Kula et al. Consecutive use of ω-aminoalkylagaroses. Resolution and purification of clostripain and collagenase from Clostridium histolyticum
Chou et al. Separation of human renal renin and pseudorenin by affinity chromatography on hemoglobin-sepharose-2B
Gubensek et al. Rapid isolation of cathepsin D by affinity chromatography on the immobilized synthetic inhibitor
US4780209A (en) Process for concentrating and separating trypsin inhibitor and kallidinogenase in human urine