Hempel et al., 1982 - Google Patents
Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1)Hempel et al., 1982
- Document ID
- 510433057095891789
- Author
- Hempel J
- Pietruszko R
- Fietzek P
- Joernvall H
- Publication year
- Publication venue
- Biochemistry
External Links
Snippet
Materials and Methods Protein. Human liver aldehyde dehydrogenase isoenzyme Ej was isolated as described (Hempel et al., 1982). The enzyme used for selective alkylation by iodo [l-14C] acetamide (13.1 mCi/mmol, NewEngland Nuclear) had a specific ac-tivity of …
- 102000005369 Aldehyde Dehydrogenase 0 title abstract description 15
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
- C07K14/575—Hormones
- C07K14/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Cardionatrin; Cardiodilatin
-
- 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
- C07K14/62—Insulins
-
- 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
-
- 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
- C07K14/57581—Thymosin; Related peptides
-
- 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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- 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
- C07K1/06—General 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
- C07K1/061—General 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 |
---|---|---|
Hempel et al. | Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1) | |
Hempel et al. | Aldehyde dehydrogenase from human liver: primary structure of the cytoplasmic isoenzyme | |
Johansen et al. | The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae | |
Brautigan et al. | Definition of cytochrome c binding domains by chemical modification. I. Reaction with 4-chloro-3, 5-dinitrobenzoate and chromatographic separation of singly substituted derivatives. | |
MARKOVIČ et al. | Pectinesterase: the primary structure of the tomato enzyme | |
Butler et al. | The use of maleic anhydride for the reversible blocking of amino groups on polypeptide chains | |
Zoller et al. | Affinity labeling of cAMP-dependent protein kinase with p-fluorosulfonylbenzoyl adenosine. Covalent modification of lysine 71. | |
Gerber et al. | Partial primary structure of bacteriorhodopsin: sequencing methods for membrane proteins. | |
Ishiura et al. | Studies of a calcium-activated neutral protease from chicken skeletal muscle: I. Purification and characterization | |
Zumstein et al. | Amino acid sequence of a variant pro-form of insulin-like growth factor II. | |
Hokama et al. | Snake Venom Proteinase Inhibitors: III. Isolation of Five Polypeptide Inhibitors from the Venoms of Hcmachatus haemachatus (Ringhal's Cobra) and Naja nivea (Cape Cobra) and the Complete Amino Acid Sequences of Two of Them | |
Fernandez-Luna et al. | Complete amino acid sequence of the Aspergillus cytotoxin mitogillin | |
Bai et al. | Identification of the cysteine residue of. beta.-tubulin alkylated by the antimitotic agent 2, 4-dichlorobenzyl thiocyanate, facilitated by separatio of the protein subunits of tubulin by hydrophobic column chromatography | |
Hase et al. | Complete amino acid sequence of Halobacterium halobium ferredoxin containing an Nε-acetyllysine residue | |
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 | |
Camardella et al. | Human erythrocyte glucose‐6‐phosphate dehydrogenase: Identification of a reactive lysyl residue labelled with pyridoxal 5′‐phosphate | |
Jackson et al. | Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues | |
Tamura et al. | Pig Gastric (H++ K+)-ATPase: Lys-497 Conserved in Cation Transporting ATPases is Modified with Pyridoxal 5′-Phosphate | |
Jelesarov et al. | Ferredoxin binding site on ferredoxin: NADP+ reductase: Differential chemical modification of free and ferredoxin‐bound enzyme | |
Feldman et al. | Purification and characterization of frog. alpha.-macroglobulin: receptor recognition of an amphibian glycoprotein | |
KARLSSON et al. | Variability within mammalian sorbitol dehydrogenases: The primary structure of the human liver enzyme | |
Kumar et al. | Affinity labeling of chicken liver dihydrofolate reductase by a substituted 4, 6-diaminodihydrotriazine bearing a terminal sulfonyl fluoride. | |
Manao et al. | Rabbit skeletal muscle acylphosphatase: the amino acid sequence of form Ra1 | |
HAUMONT et al. | Amino‐acid sequence of the cytochrome‐b5‐like heme‐binding domain from Hansenula anomala flavocytochrome b2 | |
Peeters et al. | Structural studies on rat prostatic binding protein: The primary structure of component C1 from subunit F |