[go: up one dir, main page]

Lääne et al., 1985 - Google Patents

Preparation of polymer‐modified enzymes of prolonged circulation times. Poly [N‐(2‐hydroxypropyl) methacrylamide]‐bound acetylcholinesterase

Lääne et al., 1985

Document ID
6996890500474037158
Author
Lääne A
Aaviksaar A
Haga M
Chytrý V
Kopeček J
Publication year
Publication venue
Die Makromolekulare Chemie: Macromolecular Chemistry and Physics

External Links

Snippet

A covalently bound complex of acetylcholinesterase with poly [N‐(2‐hydroxypropyl) methacrylamide] has been obtained, showing a 70‐fold prolongation of the acetylcholinesterase activity survival in mouse blood after intravenous injection of the …
Continue reading at onlinelibrary.wiley.com (other versions)

Classifications

    • 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)
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K47/00Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives
    • A61K47/48Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates
    • A61K47/48238Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being a protein, peptide, polyamino acid
    • A61K47/48246Medicinal preparations characterised by the non-active ingredients used, e.g. carriers, inert additives the non-active ingredient being chemically bound to the active ingredient, e.g. polymer drug conjugates the modifying agent being a protein, peptide, polyamino acid drug-peptide, protein or polyamino acid conjugates, i.e. the modifying agent being a protein, peptide, polyamino acid which being linked/complexed to a molecule that being the pharmacologically or therapeutically active agent

Similar Documents

Publication Publication Date Title
Kamisaki et al. Reduction in immunogenicity and clearance rate of Escherichia coli L-asparaginase by modification with monomethoxypolyethylene glycol.
Savoca et al. Preparation of a non-immunogenic arginase by the covalent attachment of polyethylene glycol
Richmond Purification and properties of the exopenicillinase from Staphylococcus aureus
Maeda et al. A lipophilic derivative of neocarzinostatin a polymer conjugation of an antitumor protein antibiotic
Barrett et al. The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
Drazin et al. Structure and activity of diphtheria toxin: II. Attack by trypsin at a specific site within the intact toxin molecule
Stricklin et al. Human skin fibroblast collagenase: chemical properties of precursor and active forms
Lee et al. Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor
Vincent et al. Structure-function relations and site of action of apamin, a neurotoxic polypeptide of bee venom with an action on the central nervous system
DK166966B1 (en) ANALOGY PROCEDURE FOR PREPARING IMMUNOENZYMATIC CONJUGATES
US4563349A (en) Superoxide dismutase, its immobilized form, and their production and use
Owens et al. A possible mechanism for the inhibition of plant viruses by a peptide from Phytolacca americana
Whiting et al. Purification and properties of solubilized mitochondrial δ-aminolevulinic acid synthetase and comparison with the cytosol enzyme
Scott et al. Secondary modification of cytochrome c by Neurospora crassa
Nagy et al. Identity of the active site flavin-peptide fragments from the human “A”-form and the bovine “B”-form of monoamine oxidase
Graf et al. Preparation of 125I-calmodulin with retention of full biological activity: its binding to human erythrocyte ghosts
Desbuquois et al. Independence of glucagon receptors and glucagon inactivation in liver cell membranes
Uren et al. Improvement in the therapeutic, immunological, and clearance properties of Escherichia coli and Erwinia carotovora L-asparaginases by attachment of poly-DL-alanyl peptides
Lääne et al. Preparation of polymer‐modified enzymes of prolonged circulation times. Poly [N‐(2‐hydroxypropyl) methacrylamide]‐bound acetylcholinesterase
Bodwell et al. Purification and characterization of carboxypeptidase A from rat skeletal muscle
Fehske et al. Direct demonstration of the highly reactive tyrosine residue of human serum albumin located in fragment 299–585
Cory et al. Isolation and characterization of enolase from rainbow trout (Salmo gairdnerii gairdnerii)
Ghelis et al. Activity and conformation of the alkaline form of δ-chymotrypsin studied by the specific acylation of isoleucine-16
Hadley et al. Catalytic activity of administered gulonolactone oxidase polyethylene glycol conjugates
Guha et al. Lobster muscle aldolase: Isolation, properties and primary structure at the substrate-binding site