Zobrazeno 1 - 10
of 12
pro vyhledávání: '"B M, Merrill"'
Autor:
Samuel H. Wilson, C J Luneau, B M Merrill, Kenneth R. Williams, Aseem Kumar, Richard L. Karpel, J R Casas-Finet
Publikováno v:
Journal of Biological Chemistry. 265:17094-17100
A1 is a core protein of the eukaryotic heterogeneous nuclear ribonucleoprotein complex and is under study here as a prototype single-stranded nucleic acid-binding protein. A1 is a two-domain protein, NH2-terminal and COOH-terminal, with highly conser
Publikováno v:
The Journal of biological chemistry. 275(39)
We have engineered a cysteine residue at position 442 (EU/OU numbering) in the third constant domain (C(H)3) of the heavy chain of several IgGs with different specificities, isoforms, and variants with the intent to introduce a site for chemical conj
Publikováno v:
Journal of bacteriology. 178(9)
A previously identified intracellular proteolytic activity in the hyperthermophilic archaeon Pyrococcus furiosus (I. I. Blumentals, A. S. Robinson, and R. M. Kelly, Appl. Environ. Microbiol. 56:1992-1998, 1990) was found to be a homomultimer consisti
Publikováno v:
Journal of anatomy. 183
The adrenal medulla chromaffin vesicle (CV) contains, on a weight basis, as much soluble protein and peptide as catecholamine. The bulk of the protein is accounted for by chromogranins (Cgr) A, B and C. Additionally, a large variety of neuropeptides
Publikováno v:
The Journal of biological chemistry. 268(14)
CaM kinase-Gr is a Ca2+/calmodulin-dependent protein kinase that is enriched in brain and thymus. The enzyme was isolated from rat cerebellum, which contained alpha (M(r) 65,000) and beta (M(r) 67,000) polypeptides, and rat forebrain, which contained
The gene coding for the Escherichia coli enzyme 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase has been cloned and sequenced. This gene, designated folK, codes for a protein of 159 amino acids, including an amino-terminal methionine. The protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c2cbb8ae84326ba3981e964370ea18f
https://europepmc.org/articles/PMC207135/
https://europepmc.org/articles/PMC207135/
Publikováno v:
The Journal of biological chemistry. 267(8)
Uracil analogues with appropriate substituents at the 5-position inactivated dihydropyrimidine dehydrogenase (DHPDHase). The efficiency of these inactivators was highly dependent on the size of the 5-substituent. For example, 5-ethynyluracil inactiva
Publikováno v:
The Journal of biological chemistry. 266(30)
5-Iodouracil was a substrate for bovine liver dihydropyrimidine dehydrogenase (DHPDHase) and was a potent inactivator of the enzyme. NADPH increased the rate of inactivation and thymine protected against inactivation. These findings suggest that 5-io
Autor:
A, Kumar, J R, Casas-Finet, C J, Luneau, R L, Karpel, B M, Merrill, K R, Williams, S H, Wilson
Publikováno v:
The Journal of biological chemistry. 265(28)
A1 is a core protein of the eukaryotic heterogeneous nuclear ribonucleoprotein complex and is under study here as a prototype single-stranded nucleic acid-binding protein. A1 is a two-domain protein, NH2-terminal and COOH-terminal, with highly conser
Publikováno v:
The Journal of biological chemistry. 261(2)
Two single-stranded nucleic acid-binding proteins, UP1 and UP2, that were originally reported by Herrick and Alberts (Herrick, G., and Alberts, B. (1976) J. Biol. Chem. 251, 2124-2132) have been purified to apparent homogeneity from calf thymus by hi