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

Kruiswijk et al., 1974 - Google Patents

Analysis of the protein composition of yeast ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis

Kruiswijk et al., 1974

Document ID
16837727370152262466
Author
Kruiswijk T
Planta R
Publication year
Publication venue
Molecular biology reports

External Links

Snippet

The number of proteins in yeast ribosomal subunits was determined by two-dimensional polyacrylamide gel electrophoresis. The 40S subunit obtained after dissociation of ribosomes at high ionic strength contains 30 different protein species (including six acidic …
Continue reading at link.springer.com (other versions)

Classifications

    • 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
    • C07K14/47Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • 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
    • C07K14/43504Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N27/00Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means
    • G01N27/26Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
    • G01N27/416Systems
    • G01N27/447Systems using electrophoresis
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • 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
    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • 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
    • C07K1/24Extraction; Separation; Purification by electrochemical means
    • 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
    • C07K1/06General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents
    • C07K1/061General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using protecting groups

Similar Documents

Publication Publication Date Title
Kruiswijk et al. Analysis of the protein composition of yeast ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis
Jacobson et al. Abundance and membrane association of elongation factor Tu in E. coli
Schmitges et al. The major proteins of the Escherichia coli outer cell‐envelope membrane. Heterogeneity of protein I
Nicholson et al. Rat liver gap junction protein: properties and partial sequence.
Véron et al. The Threonine‐Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12: The Two Catalytic Activities Are Carried by Two Independent Regions of the Polypeptide Chain
WILK et al. The core proteins of 35 s hnRNP complexes: characterization of nine different species
Goldman et al. Bacillus subtilis spore coats: complexity and purification of a unique polypeptide component
Greer et al. Actin from Saccharomyces cerevisiae
Marriq et al. Polypeptide chains of 19‐S thyroglobulin from several mammalian species and of porcine 27‐S iodoprotein
Herbrink et al. Further studies on the polypeptide chains of β-crystallin
Schmitz et al. Genetic studies of the lac repressor: V. Repressors which bind operator more tightly generated by suppression and reversion of nonsense mutations
Witheiler et al. The purification and characterization of a novel peptidase from sheep red cells
Durrens The phenoloxidases of the ascomycete Podospora anserina: the three forms of the major laccase activity
Penneys et al. Human placental tryptophanyl transfer ribonucleic acid synthetase. Purification and subunit structure
Bretscher Direct translation of bacteriophage fd DNA in the absence of neomycin B
OLAFSON Prokaryotic metallothionein: amino terminal sequence analysis of a unique metallothionein
Coddington et al. Characterisation of the ribosomal proteins from Schizosaccharomyces pombe by two-dimensional polyacrylamide gel electrophoresis: Demonstration that a cycloheximide resistant strain, cyh 1, has an altered 60S ribosomal protein
Low et al. Skeletal muscle ribosomal proteins: general characteristics and effect of diabetes
Turner et al. Mitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein
Yaguchi et al. Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli: II. Localization of amino acid replacements in proteins S5 and S12 altered in double mutants resistant to neamine
Ono et al. Yeast UAA suppressors effective in ψ+ strains: Leucine-inserting suppressors
Kahan et al. The structural gene for the ribosomal protein S18 in Escherichia coli: II. Chemical studies on the protein S18 having an altered electrophoretic mobility
Kolodrubetz et al. Amino‐terminal sequence of a Saccharomyces cerevisiae nuclear protein, NHP6, shows significant identity to bovine HMG1
Harper et al. The hydrolysis of poly (L‐prolyl‐glycyl‐L‐prolyl) by bacterial collagenase
Lambertsson The ribosomal proteins of Drosophila melanogaster: II. Comparison of protein patterns of ribosomes from larvae, pupae and adult flies by two-dimensional polyacrylamide gel electrophoresis