Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid.

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Abstract Text:

S Hashimoto,S Takemura,S Yabuki,K Konishi,T Samejima,

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Publishing Authors By Initials

S Hashimoto,S Takemura,S Yabuki,K Konishi,T Samejima,

For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research

PUBMED ID PMID:

MEDLINE DATE:

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 72

Page Numbers: 1185-95

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1972

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Keywords Mesh Terms:

KEYWORDS: Tyrosine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid. Information

Substance Name: Nucleotidyltransferases

Registry Number: EC 2.7.7.-

Grant and Affiliation Information for Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid Related Publications

• Bindings of Ca2+ ion and monodispersed n-alkylphosphorylcholines to phospholipase A2-II of A. halys blomhoffii.
• Changes of thermostability and activity of thermolysin on nitration with tetranitromethane.
• Comparative studies on the primary structure of human cystatin as from epidermis, liver, spleen, and leukocytes.
• Conformational changes of papain induced on interaction with thiol proteinase inhibitors from newborn rat epidermis.
• DTNB modification of SH groups of isocitrate dehydrogenase from Bacillus stearothermophilus purified by affinity chromatography.
• Dissociation of bovine liver catalase into subunits on acetylation.
• Effect of sodium dodecyl fulfate on the dissociation of bovine liver catalase.
• Effects of divalent cations on thermophilic inorganic pyrophosphatase.
• Effects of halide ions on porcine kidney catalase.
• Formation of spermidine or norspermidine from synthetic diacetylpolyamines by acetylpolyamine oxidase in cultured cells.
• Isolation and characterization of two thiol proteinase inhibitors of low molecular weight from newborn rat epidermis.
• Monospecific antiserum to rat spermidine synthase and its application to rat tissues and several mammals.
• On the characterization of porcine erythrocyte catalase and its disulfide-linked dimer.
• On the conformation of NADP-dependent isocitrate dehydrogenase from Bacillus stearothermophilus.
• On the denaturation of porcine erythrocyte catalase with alkali, urea, and guanidine hydrochloride in relation to its subunit structure.
• On the heterogeneity of catalase from goat liver. Purification and characterization.
• Physico-chemical studies on conformation of a complex reconstituted from half molecules of Torulopsis utilis tyrosine transfer ribonucleic acid.
• Purification and characterization of inorganic pyrophosphatase from Bacillus stearothermophilus.
• Some chemical and physical properties of ribonuclease from Aspergillus saitoi.
• Some properties of glutamine synthetase from baker's yeast.
• Studies on chemical synthesis of human cystatin A gene and its expression in Escherichia coli.
• Subcellular distribution and characterization of porcine kidney catalase.
• Substrate recognition by glycoside hydrolase family 74 xyloglucanase from the basidiomycete Phanerochaete chrysosporium.
• The change of stability and activity of thermolysin by acetylation with N-acetylimidazole.
• The interactions of thiol compounds with porcine erythrocyte catalase.
• The modification of sulfhydryl groups of glutamine synthetase from Bacillus stearothermophilus with 5, 5'-dithiobis(2-nitrobenzoic acid).
• The specific modification of histidyl residues of inorganic pyrophosphatase from Bacillus stearothermophilus by photooxidation.
• pH dependence of the binding constant of Ca2+ to the phospholipase A2 of A. halys blomhoffii. Participation of ionizable groups with pK values of 5.16, 6.45, and 7.30.
• pH dependence of the binding constant of a phospholipase A2 from Agkistrodon halys blomhoffii venom to micelles of n-hexadecylphosphorylcholine.
• pH-dependence of the binding constant of monodispersed n-dodecylphosphorylcholine to the phospholipase A2 of A, Halys blomhoffii. Participation of ionizable groups with pK of 5.16 and 7.30.