Crystalline leucine aminopeptidase from lens (alpha-aminoacyl-peptide hydrolase; EC 3.4.11.1). 1976

H Henson, and M Frohne

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D007908 Lens, Crystalline A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION. Eye Lens,Lens, Eye,Crystalline Lens
D007931 Leucyl Aminopeptidase A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. Cytosol Aminopeptidase,Leucine Aminopeptidase,L-Leucylnaphthylamidase,Methoxyleucine Aminopeptidase,Peptidase S,Zinc-Manganese-Leucine Aminopeptidase,Aminopeptidase, Cytosol,Aminopeptidase, Leucine,Aminopeptidase, Leucyl,Aminopeptidase, Methoxyleucine,Aminopeptidase, Zinc-Manganese-Leucine,Zinc Manganese Leucine Aminopeptidase
D008722 Methods A series of steps taken in order to conduct research. Techniques,Methodological Studies,Methodological Study,Procedures,Studies, Methodological,Study, Methodological,Method,Procedure,Technique
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009905 Optical Rotatory Dispersion The method of measuring the dispersion of an optically active molecule to determine the relative magnitude of right- or left-handed components and sometimes structural features of the molecule. Dispersion, Optical Rotatory,Rotatory Dispersion, Optical
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002413 Cations, Divalent Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis. Divalent Cations
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism

Related Publications

H Henson, and M Frohne
November 1967, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Henson, and M Frohne
January 1971, Biokhimiia (Moscow, Russia),
H Henson, and M Frohne
November 1962, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Henson, and M Frohne
February 1969, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Henson, and M Frohne
November 1968, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
H Henson, and M Frohne
November 1962, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
Copied contents to your clipboard!