scholarly journals The bovine plasma retinol-binding protein. Amino acid sequence, interaction with transthyretin, crystallization and preliminary X-ray data

1990 ◽  
Vol 192 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Rodolfo BERNI ◽  
Monica STOPPINI ◽  
Maria Carla ZAPPONI ◽  
Maria Laura MELONI ◽  
Hugo L. MONACO ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Amino Acid ◽  
X Ray ◽  
Protein Amino Acid Sequence ◽  
Bovine Plasma ◽  
Plasma Retinol

scholarly journals The subunit structure of prealbumin

1971 ◽  
Vol 125 (1) ◽  
pp. 309-317 ◽  
Author(s):  
G. Gonzalez ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Quaternary Structure ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Subunit Structure ◽  
Sequence Determination ◽  
Tryptic Peptides ◽  
X Ray

1. Prealbumin, a thyroxine-binding protein, is known to bind also to retinol-binding protein and is suspected on X-ray-crystallographic evidence of having a quaternary structure. 2. Experiments described in this paper suggest that the molecule is a tetramer of mol.wt. about 56000, which is disaggregated with some difficulty into subunits of mol.wt. about 14000. 3. The number and staining properties of the tryptic peptides indicate that the subunits are identical or closely similar. This conclusion is reinforced by comparing the sum of the amino acid compositions of the tryptic peptides with the amino acid composition of the whole protein. All minor peptides that were isolated could be shown to be derived from major peptides. 4. No evidence has been found, either from electrophoretic experiments or from amino acid sequence determination, for any dissimilarity between the subunits.

Computer prediction of potential immunogenic determinants from protein amino acid sequence

1987 ◽  
Vol 165 (1) ◽  
pp. 200-207 ◽  
Author(s):  
Viktor Krchňák ◽  
Otakar Mach ◽  
Antonín Malý
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Amino Acid ◽  
Computer Prediction ◽  
Protein Amino Acid Sequence

Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self-Association

1990 ◽  
Vol 55 (3) ◽  
pp. 950-955 ◽  
Author(s):  
Trudy J. Milne ◽  
Annette R. Atkins ◽  
Juanita A. Warren ◽  
Wendy P. Auton ◽  
Ross Smith
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Amino Acid ◽  
Protein Amino Acid Sequence ◽  
Self Association

scholarly journals Retinol binding protein 4 in dairy cows: its presence in colostrum and alteration in plasma during fasting, inflammation, and the peripartum period

2009 ◽  
Vol 77 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Mabrouk A Abd Eldaim ◽  
Akihiro Kamikawa ◽  
Mohamed M Soliman ◽  
Mohamed M Ahmed ◽  
Yuko Okamatsu-Ogura ◽  
...  
Keyword(s):  
Dairy Cows ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Retinol Binding Protein 4 ◽  
Lps Challenge ◽  
Bovine Plasma ◽  
Basal Plasma ◽  
Peripartum Period ◽  
Plasma Retinol ◽  
Retinol Concentration

Retinol-binding protein 4 (RBP4) is a plasma protein involved in retinol transportation, and recent evidence in rodents suggests that RBP4 is also a metabolic regulator that modifies insulin sensitivity. To assess how RBP4 levels are regulated in ruminants, we determined the RBP4 concentrations in bovine plasma and milk using Western blot analysis. Plasma RBP4 levels in non-pregnant non-lactating (control) cows were around 45 μg/ml, which were sustained during 60-h fasting, but decreased significantly 4 h after lipopolysaccharide (LPS) administration. Basal plasma retinol concentration was around 30 μg/dl, but this decreased to approximately one-third and one-half of these values during fasting and 8 h after LPS challenge, respectively. Plasma RBP4 and retinol levels in cows 3–6 d before parturition were comparable to those of the controls. However, on the day of parturition both were significantly decreased and had returned to basal levels by two weeks after calving. Interestingly, RBP4 was clearly detected in colostrum (16·4±5·6 μg/ml) but was only faintly detected in milk from cows at 7 d and 15 d after calving. Retinol concentrations in colostrum were almost 10-fold higher than those in plasma, while those in milk were comparable to those in plasma. These results suggest that RBP4 and retinol levels are independently regulated under physiological and pathophysiological conditions and that RBP4, like retinol, is transferred from maternal stores to calves through colostrum.

Correlation of the β-sheet crystal size in silk fibers with the protein amino acid sequence

Soft Matter ◽  
2007 ◽  
Vol 3 (7) ◽  
pp. 877-882 ◽  
Author(s):  
Lawrence F. Drummy ◽  
B. L. Farmer ◽  
Rajesh R. Naik
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Crystal Size ◽  
Protein Amino Acid ◽  
Silk Fibers ◽  
Protein Amino Acid Sequence ◽  
Β Sheet

Detection of Protein Coding Sequences Using a Mixture Model for Local Protein Amino Acid Sequence

2000 ◽  
Vol 7 (1-2) ◽  
pp. 317-327 ◽  
Author(s):  
Edward C. Thayer ◽  
Chris Bystroff ◽  
David Baker
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mixture Model ◽  
Protein Amino Acid ◽  
Protein Coding ◽  
Coding Sequences ◽  
Protein Amino Acid Sequence ◽  
Local Protein
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