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

Ooi et al., 1963 - Google Patents

Structural studies of ribonuclease. VIII. Tryptic hydrolysis of ribonuclease A at elevated temperatures

Ooi et al., 1963

Document ID
1982686788664493371
Author
Ooi T
Rupley J
Scheraga H
Publication year
Publication venue
Biochemistry

External Links

Snippet

Method.—Digestion of ribonuclease A with trypsin was carried out in 0.01 M KC1, pH 6.5, 60, in a pH stat (Radiometer 1) as described in the previous paper (Rupley and Scheraga, 1963). A concentration of ribonuclease A of 10 mg/ml was used routinely. Trypsin loses its …
Continue reading at pubs.acs.org (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)
    • C12N9/48—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
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
    • 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)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • 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
    • 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
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81—Protease inhibitors
    • 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
    • C07K1/12—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by hydrolysis, i.e. solvolysis in general

Similar Documents

Publication Publication Date Title
Ooi et al. Structural studies of ribonuclease. VIII. Tryptic hydrolysis of ribonuclease A at elevated temperatures
Udenfriend et al. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
Matsubara et al. Specific nature of hydrolysis of insulin and tobacco mosaic virus protein by thermolysin
MacGregor et al. The degradation of proparathormone and parathormone by parathyroid and liver cathepsin B.
Bustin et al. Bisection of a lysine-rich histone by N-bromosuccinimide
Eisen et al. Collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. Purification and properties
Hunt et al. Abnormal human haemoglobins VI. The chemical difference between haemoglobins A and E
Shapira et al. Encephalitogenic fragment of myelin basic protein: amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments
Allende et al. The action of trypsin on ribonuclease-S
Evenberg et al. Amino acid sequence of phospholipase A2 from horse pancreas.
Reeck et al. Isolation and characterization of pancreatic procarboxypeptidase B and carboxypeptidase B of the African lungfish
Marinkovic et al. Purification of carboxypeptidase B from human pancreas
Fujikawa et al. A comparison of bovine prothrombin, factor IX (Christmas factor), and factor X (Stuart factor)
Fellows Jr et al. Structural Studies on Bovine Growth Hormone: I. Isolation and characterization of cyanogen bromide fragments
Hofmann The purification and properties of fragments of trypsinogen obtained by cyanogen bromide cleavage
Pedersen et al. The amino acid sequence of a hitherto unobserved segment from porcine pepsinogen preceeding the N-terminus of pepsin
Perham et al. The Determination of the Order of Lysine‐containing: Tryptic Peptides of Proteins by Diagonal Paper Electrophoresis A Carboxyl‐terminal Sequence for Pepsin
Keller et al. The preparation of purified collagenase
Bromer et al. The amino acid sequence of glucagon. III. The hydrolysis of glucagon by trypsin
Shechter et al. Selective reduction of cystine I-VIII in α-lactalbumin of bovine milk
Heinrickson et al. [64] Acidic systeine protease inhibitors from pineapple stem
Morgan et al. The structure of streptokinase I. Cyanogen bromide fragmentation, amino acid composition and partial amino acid sequences
Sanger Some chemical investigations on the structure of insulin
Doonan et al. The primary structure of aspartate aminotransferase from pig heart muscle determined in part using a protease with specificity for lysine
Kress et al. The Basic Trypsin Inhibitor of Bovine Pancreas: IX. LOCATION OF THE REACTIVE SITE IN THE CARBOXAMIDOMETHYL DERIVATIVE