scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-Bisphosphatase. I. The S-Peptide

1980 ◽  
Vol 33 (6) ◽  
pp. 665 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Electrophoresis ◽  
Fructose Bisphosphatase ◽  
Purification Step ◽  
Sheep Liver ◽  
Final Purification Step ◽  
Elution Chromatography ◽  
Final Purification

Fructose-bisphosphatase has been isolated from sheep liver using affinity-elution chromatography from carboxymethykellulose as the final purification step. The purified enzyme was homogeneous by disc gel electrophoresis.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

scholarly journals The EGD1 product, a yeast homolog of human BTF3, may be involved in GAL4 DNA binding.

1992 ◽  
Vol 12 (12) ◽  
pp. 5683-5689 ◽  
Author(s):  
M R Parthun ◽  
D A Mangus ◽  
J A Jaehning
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Yeast Cells ◽  
Stable Complex ◽  
Affinity Column ◽  
Gene Encoding ◽  
Heat Stable ◽  
Gel Retardation ◽  
Final Purification Step

A variety of techniques, including filter binding, footprinting, and gel retardation, can be used to assay the transcriptional activator GAL4 (Gal4p) through the initial steps of its purification from yeast cells. Following DNA affinity chromatography, Gal4p still bound DNA selectively when assayed by filter binding or footprinting. However, the affinity-purified protein was no longer capable of forming a stable complex with DNA, as assayed by gel retardation. Mixing the purified Gal4p with the flowthrough fraction from the DNA affinity column restored gel retardation complex formation. Gel retardation assays were used to monitor the purification of a heat-stable Gal4p-DNA complex stabilization activity from the affinity column flowthrough. The activity coeluted from the final purification step with polypeptides of 21 and 27 kDa. The yeast gene encoding the 21-kDa protein was cloned on the basis of its N-terminal amino acid sequence. The gene, named EGD1 (enhancer of GAL4 DNA binding), encodes a highly basic protein (21% lysine and arginine) with a predicted molecular mass of 16.5 kDa. The amino acid sequence of the EGD1 product, Egd1p, is highly similar to that of the human protein BTF3 (X. M. Zheng, D. Black, P. Chambon, and J. M. Egly, Nature [London] 344:556-559, 1990). Although an egd1 null mutant was viable and Gal+, induction of the galactose-regulated genes in the egd1 mutant strain was significantly reduced when cells were shifted from glucose to galactose.

Isolation and in vitro translation of mRNA from the calf abomasal mucosa and identification of an mRNA coding for a precursor of prochymosin

1984 ◽  
Vol 51 (1) ◽  
pp. 79-89
Author(s):  
Bruce H. Nicholson ◽  
Peter Jones
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Electrophoresis ◽  
Signal Sequence ◽  
In Vitro Translation ◽  
Major Band ◽  
Polyadenylated Rna ◽  
Age Related

SummaryThe mRNA coding for prochymosin (prorennin) has been partly purified from calf abomasum. The in vitro translation products of the total polyadenylated RNA show a major band on gel electrophoresis which reacts with antibody raised against purified chymosin. The mol. wt of 43000 is higher than expected from the reported amino acid sequence and would correspond to prochymosin with an unprocessed signal sequence of ∼ 17 amino acids. The synthesis of chymosin mRNA is age-related, and ceases by 3 months even in milk-fed calves.

scholarly journals Genetic variants involving the major membrane sialoglycoprotein of human erythrocytes. Studies on erythrocytes of type Mk, Miltenberger class V and Mg

1978 ◽  
Vol 175 (1) ◽  
pp. 149-157 ◽  
Author(s):  
D J Anstee ◽  
M J A Tanner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Blood Group ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Membrane Component ◽  
Class V ◽  
Normal Cells ◽  
Antigenic Properties

1. Membranes from erythrocytes heterozygous for the Mk and Miltenberger Class V (Mi.V) condition and membranes from erythrocytes homozygous for the Mg condition were studied by polyacrylamide-gel electrophoresis by using the periodate/Schiff stain binding of radioiodinated lectins and labelling with lactoperoxidase. 2. Both the Mk and Mi.V conditions are associated with a decreased content of the major blood-group-MN-active sialoglycoprotein. 3. An unusual blood-group-M-active membrane component was found in Mi.V cells of appropriate genotype. No comparably component was found in Mk erythrocytes. 4. The Mg antigen appears to result from a modification of the MN-active sialoglycoprotein found in normal cells. Our results suggest that the Mg sialoglycoprotein contains fewer sialotetrasaccharides than does the normal sialglycoprotein. This may result from changes in the amino acid sequence of the protein. 5. The results are discussed in relation to differences in the antigenic properties of Mk, Mi.V and Mg cells and their possible influence on the structure of the surface of each of these cells.

Sign in / Sign up

Export Citation Format

Share Document