Isolation, purification, and crystallization of aspartate aminotransferase from wheat grain.

A procedure for isolation and purification of aspartate aminotransferase from wheat grain includes chromatography on DEAE cellulose, acidification-alkalization, precipitation with protamine sulfate, fractionation with ammonium sulfate, and chromatography on hydroxyapatite. The yield of protein was 27% with 95% purity. Crystals of the enzyme (0.

[A new form of aspartate aminotransferase crystals].

A new crystal form of chicken cytosolic aspartate aminotransferase (EC 2.6.1.

[The complex of aspartate aminotransferase with D-aspartate].

We report here the x-ray studies of the complex cytosolic aspartate aminotransferase from chicken heart with D-aspartate at 2,7 A resolution. Crystals of the complex was prepared by diffusing D-aspartate into free enzyme crystals; their space group is P 2(1)2(1)2(1) with cell dimensions (A): a = 62.59; b = 117.

[Study of crystals of aspartate aminotransferase complexed with D-aspartate].

We report here the first X-ray studies of the complex of cytosolic aspartate aminotransferase from chicken heart with D-aspartate at 2.5 A resolution. Crystals of the complex were grown by cocrystallization (space group is P2(1)2(1)2(1), parameters: a = 62.

[Crystals of free aspartate aminotransferase].

The crystals of free cytosolic chicken aspartate aminotransferase were subjected to X-ray investigation at 2.7 A. One subunit of the dimeric molecule crystalline enzyme is in the open conformation and the other is in the closed conformation.

[The existence of the ribonucleoprotein branching enzyme in rabbit skeletal muscle and ribozyme corresponding to it].

Amylose isomerase (AI) preparations were isolated from rabbit muscles after Petrova et al., as well as by the additional fractionation steps. Their homogeneity, enzymatic activity and RNA, isolated from those preparations, were characterized.

[Crystallization of free aspartate aminotransferase from chicken heart cytosol].

Homogeneous aspartate aminotransferase (purity--99%, yield--70%) has been prepared from chicken heart cytosol. The purification procedure included fractionation with ammonium sulfate and ethanol and crystallization. Crystals (0.

[Isolation and characteristics of insulin-binding proteins from soybeans].

Two soybean insulin-binding proteins were isolated using affinity chromatography on insulin-Sepharose. Both proteins have molecular mass about 39 kDa and consist of two subunits linked by disulphide bonds. According to the amino acid composition and N-terminal sequences of the subunits, these proteins, characterized by the absence of free thiol groups and sugar residues, are variants of the previously described soybean basic 7S globulin.

[Catalytic properties of aspartate aminotransferase].

Analysis of Michaelis--Menten kinetics revealed that the enzyme in solution and the crystalline cytosolic aspartate aminotransferase (EC 2.6.1.

[Spectral properties of aspartate transaminase from chicken heart cytosol].

For the first time an interaction between aspartate transaminase (EC 2.6.1.

[Cytosol aspartate aminotransferase from the chicken heart: three-dimensional structure at 2.8 angstroms resolution and the characteristic conformation of various enzyme forms].

The spatial structure of cytosolic chicken aspartate aminotransferase (AAT) has been determined by X-ray crystallographic analysis at 2.8 A resolution. AAT consists of two chemically identical subunits.

Reorientations of coenzyme in aspartate transaminase studied on single crystals of the enzyme by polarized-light spectrophotometry.

Investigation of polarized-light absorption spectra of single crystals of cytosolic aspartate transaminase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.

[Improved procedure for purification of aspartate transaminase from chicken heart cytosol. Characterization of the enzyme].

The purification procedure reported includes fractionation of water extract from chicken hearts with ammonium sulfate, fractional precipitation with ethanol, chromatography on Whatman CM-52 cellulose and crystallization. Specific activity of the pure crystalline enzyme was 234 micromoles.min-1.