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

Bonnet et al., 1992 - Google Patents

Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide

Bonnet et al., 1992

View PDF
Document ID
8367561383570576280
Author
Bonnet F
Perin J
Maillet P
Jolles P
Alliel P
Publication year
Publication venue
Biochemical Journal

External Links

Snippet

A glycosaminoglycan-bearing polypeptide (S. GP), present in human seminal plasma, was purified to homogeneity by a combination of CsCl density-gradient centrifugation, fplc ion- exchange chromatography on a Mono Q HR column and Superose 6 gel filtration. The …
Continue reading at www.ncbi.nlm.nih.gov (PDF) (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
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4702—Regulators; Modulating activity
    • 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
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • 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
    • C07K14/8139—Cysteine protease (E.C. 3.4.22) inhibitors, e.g. cystatin
    • 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)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • 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)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/14—Extraction; Separation; Purification
    • C07K1/16—Extraction; Separation; Purification by chromatography
    • C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes
    • 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
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0089—Oxidoreductases (1.) acting on superoxide as acceptor (1.15)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Similar Documents

Publication Publication Date Title
Bonnet et al. Characterization of a human seminal plasma glycosaminoglycan-bearing polypeptide
Thorne et al. The structure of ubiquitinated histone H2B.
Clarke et al. The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzyme C
Goodwin et al. Isolation and characterisation of two calf‐thymus chromatin non‐histone proteins with high contents of acidic and basic amino acids
Moorhead et al. Purification of type 1 protein (serine/threonine) phosphatases by microcystin‐Sepharose affinity chromatography
EP0528820B1 (en) Methods and compositions for the identification, characterization and inhibition of farnesyl protein transferase
Foltmann et al. Human progastricsin: analysis of intermediates during activation into gastricsin and determination of the amino acid sequence of the propart
Odani et al. Purification and complete amino acid sequence of novel β2-microglobulin
Otterson et al. Stch encodes the ‘ATPase core’of a microsomal stress 70 protein.
Sidler et al. The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase
Hnilica Studies on nuclea proteins I. Observations on the tissue and species specificity of the moderately lysine-rich histone fraction 2b
Van Patten et al. Molecular cloning of a rat testis form of the inhibitor protein of cAMP-dependent protein kinase.
Johnson et al. Factor D of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site
AU615635B2 (en) Antistasin having anticoagulant and antimetastatic properties
Escribano et al. Isolation and cytotoxic properties of a novel glycoconjugate from corms of saffron plant (Crocus sativus L.)
Brandt et al. The histones of yeast: the isolation and partial structure of the core histones
Reid et al. Human C4-binding protein: N-terminal amino acid sequence analysis and limited proteolysis by trypsin
Bennett et al. UV-catalyzed cross-linking of Escherichia coli uracil-DNA glycosylase to DNA. Identification of amino acid residues in the single-stranded DNA binding site.
Schultes et al. Complete amino‐acid sequence of glyceraldehyde‐3‐phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
YIN et al. Pseudomonas 3β‐hydroxysteroid dehydrogenase: Primary structure and relationships to other steroid dehydrogenases
CA2143621C (en) Horseshoe crab amebocyte lysate factor g subunit a and dna encoding thereof
VAN DAMME et al. Type 1 ribosome-inactivating proteins are the most abundant proteins in iris (Iris hollandica var. Professor Blaauw) bulbs: characterization and molecular cloning
Tsunasawa et al. [46] Acylamino acid-releasing enzyme from rat liver
Kanaya et al. Comparison of the primary structures of ribonuclease U2 isoforms
Valbonesi et al. Preparation of highly purified momordin II without ribonuclease activity