Zobrazeno 1 - 9
of 9
pro vyhledávání: '"C E, Argaraña"'
Publikováno v:
Genetica. 105(3)
A sequence similar to prokaryotic transposable elements was identified in the long 5' untranslated region (5'UTR) of the butanediol dehydrogenase cDNA isolated from a bovine brain lambda gt11 library. Several observations suggested that this sequence
Publikováno v:
Human mutation. 12(5)
While screening for new mutations in the HEXB gene, which encodes the beta-subunit of beta-hexosaminidase, a TG deletion (deltaTG) was found in the 3' untranslated region (3'UTR) of the gene, 7 bp upstream from the polyadenylation signal. Examination
Publikováno v:
Molecular and cellular biochemistry. 170(1-2)
A preparation of tubulin carboxypeptidase partially purified from bovine brain was found to contain a protein of molecular mass 30 kDa (P30) as determined by SDS-PAGE, that is recognized by a polyclonal anti-bovine pancreatic carboxypeptidase A. Howe
Autor:
M, González, L A, Bagatolli, I, Echabe, J L, Arrondo, C E, Argaraña, C R, Cantor, G D, Fidelio
Publikováno v:
The Journal of biological chemistry. 272(17)
The effect of biotin binding on streptavidin (STV) structure and stability was studied using differential scanning calorimetry, Fourier transform infrared spectroscopy (FT-IR), and fluorescence spectroscopy. Biotin increases the midpoint temperature
Publikováno v:
Medicina. 55(3)
Publikováno v:
Biochemistry international. 28(5)
It was found that the detyrosination of tyrosinated tubulin by tubulin carboxypeptidase can occur when both the enzyme and the substrate are adsorbed on nitrocellulose. This, and the use of a specific antibody that recognizes detyrosinated tubulin al
Publikováno v:
The Journal of biological chemistry. 256(2)
Rat brain extracts contain two heat-stable, nondialyzable inhibitors of tubulinyl-tyrosine carboxypeptidase. One of the inhibitors was sensitive to ribonuclease and insensitive to trypsin and pronase, indicating that the inhibitor is RNA. This is sup
Publikováno v:
Journal of neuroscience research. 12(4)
When a 25-50% ammonium-sulphate-insoluble fraction from a bovine brain preparation was chromatographed on a cellulose phosphate column, several protein fractions which inhibit the activity of tubulinyl-tyrosine carboxypeptidase were obtained. One of
Publikováno v:
The Journal of biological chemistry. 262(29)
We have characterized a streptavidin product that had been reduced to a minimal size that still retained full biotin-binding activity. This core streptavidin is proteolyzed at both ends at points that correspond closely with the termini of hen egg wh