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

Arlaud et al., 1983 - Google Patents

Complete amino acid sequence of the catalytic chain of human complement subcomponent C. hivin. 1r

Arlaud et al., 1983

Document ID
17215579427095078147
Author
Arlaud G
Gagnon J
Publication year
Publication venue
Biochemistry

External Links

Snippet

Gérard J. Arlaud* and Jean Gagnon abstract: The amino acidsequence of human Clr b chain has been determined, from sequence analysis performed on fragments obtained by CNBr cleavage, dilute acid hydrolysis, tryptic cleavage of the succinylated protein, and …
Continue reading at pubs.acs.org (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81—Protease inhibitors
    • C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/575—Hormones
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/914—Hydrolases (3)
    • G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
    • G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
    • G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
    • G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
    • G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies

Similar Documents

Publication Publication Date Title
Arlaud et al. Complete amino acid sequence of the catalytic chain of human complement subcomponent C. hivin. 1r
Sekiguchi et al. Domain structure of hamster plasma fibronectin. Isolation and characterization of four functionally distinct domains and their unequal distribution between two subunit polypeptides.
Bjarnason et al. Kallikrein-like enzymes from Crotalus atrox venom.
Tack et al. [7] The third, fourth, and fifth components of human complement: Isolation and biochemical properties
Butkowski et al. Primary Structure of Human Prethrombin 2 and cw-Thrombin
Harrison Human C. lovin. 1 inhibitor: improved isolation and preliminary structural characterization
AU635007B2 (en) Matrix metalloproteinase peptides: role in diagnosis and therapy
Beintema et al. Amino acid sequence of the nonsecretory ribonuclease of human urine
De Caro et al. Complete amino acid sequence of an immunoreactive form of human pancreatic stone protein isolated from pancreatic juice
KR100259759B1 (en) Inhibitors of thrombin
Dela et al. The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc‐dependent binding to an anionic surface
Kuo et al. Amino acid sequence and characterization of a heparin-binding neurite-promoting factor (p18) from bovine brain.
Chang The hirudin-binding site of human α-thrombin: identification of lysyl residues which participate in the combining site of hirudin-thrombin complex
Grant et al. Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator
Pirkle et al. The primary structure of crotalase, a thrombin-like venom enzyme, exhibits closer homology to kallikrein than to other serine proteases
Conlon et al. Conversion of substance P to C-terminal fragments in human plasma
Casarini et al. Angiotensin converting enzymes from human urine of mild hypertensive untreated patients resemble the N-terminal fragment of human angiotensin I-converting enzyme
AU700631B2 (en) Prothrombin derivatives
Nissen et al. Limited proteolysis of β2‐microglobulin at Lys‐58 by complement component C1s
HIRAO et al. Purification and characterization of cathepsin B from monkey skeletal muscle
Hermann et al. Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylase
Chang et al. The structural elements of hirudin which bind to the fibrinogen recognition site of thrombin are exclusively located within its acidic C-terminal tail
SCHLAEPPI et al. Preparation of monoclonal antibodies to hirudin and hirudin peptides: A method for studying the hirudin–thrombin interaction
US7078508B2 (en) Ixodes scapularis tissue factor pathway inhibitor
Arlaud et al. The catalytic chain of human complement subcomponent C 1. Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments