[go: up one dir, main page]

Steers Jr et al., 1974 - Google Patents

[34] β-Galactosidase

Steers Jr et al., 1974

Document ID
15475105450768586121
Author
Steers Jr E
Cuatrecasas P
Publication year
Publication venue
Methods in Enzymology

External Links

Snippet

Publisher Summary The enzyme β-galactosidase is one of several oligosaccharide-splitting enzymes that have been purified and subsequently characterized to varying degrees both physically and mechanistically. It is found in a wide range of biological sources in both the …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • 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
    • 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)
    • 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
    • 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
    • C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
    • C12N11/14—Enzymes or microbial cells being immobilised on or in an inorganic carrier
    • 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
    • C12N9/90—Isomerases (5.)
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00—Chemistry: molecular biology and microbiology
    • Y10S435/814—Enzyme separation or purification
    • Y10S435/815—Enzyme separation or purification by sorption
    • 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
    • C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
    • C12N11/02—Enzymes or microbial cells being immobilised on or in an organic carrier

Similar Documents

Publication Publication Date Title
Steers et al. The purification of β-galactosidase from Escherichia coli by affinity chromatography
US3917527A (en) Hydrophobic chromatography
Cuatrecasas et al. Selective enzyme purification by affinity chromatography.
Wilchek et al. Affinity Chromatography of Bovine Pancratic Ribonuclease A
KR100286078B1 (en) Purified Chitin Deacetylase
US8563288B2 (en) Removal of plasmin or plasminogen from cryoprecipitate
Steers Jr et al. [34] β-Galactosidase
Liao Bovine pancreatic deoxyribonuclease D
US3746622A (en) Composition and process
US4020268A (en) Agarose containing affinity matrix materials
Jensen et al. Studies on T4 lysozyme: affinity for chitin and the use of chitin in the purification of the enzyme
KR100351345B1 (en) DNA encoding chitin deacetylase
Bartkowiak et al. The purification of aminoacyl-tRNA synthetases by affinity chromatography
NEMAT‐GORGANI et al. Non‐ionic adsorptive immobilization of proteins to palmityl‐substituted Sepharose 4B
Pacaud Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase
Le Bras et al. A proteolyzed derivative of E. coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding
Sharma et al. Affinity chromatography of Ruta graveolens L. O-methyltransferases. Studies demonstrating the potential of the technique in the mechanistic investigation of O-methyltransferases
Philip et al. Rabbit muscle phosphorylase derivatives with oligosaccharides covalently bound to the glycogen storage site
Wilchek The use of affinity chromatography for the purification of affinity labeled peptides from staphylococcal nuclease
Hardesty et al. [34] Transfer factor II (T-II) from rabbit reticulocytes
Abdel Mohsen et al. Ligand-induced conformational changes of thymidylate synthase detected by limited proteolysis
Pogell et al. [32] Specific elution with substrate
Joner Purification and properties of l-asparaginase B from Acinetobacter calcoaceticus
Scott et al. Affinity chromatography purification of Clostridium perfringens enterotoxin
Grazi et al. Active subunits of rabbit liver fructose diphosphatase