Spectrofluorimetric Characterization of Serum Pentosidine and Retinol Binding Protein in Healthy Rats and Rats with Streptozotocin-Induced Diabetes

2019 ◽  
pp. 3-8
Author(s):  
D. M. Ciobanu ◽  
L. E. Olar ◽  
R. Ştefan ◽  
G. Roman ◽  
I. Papuc
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Streptozotocin Induced Diabetes

Characterization of protein production by caprine placental membranes: identification and immunolocalization of retinol-binding protein

1995 ◽  
Vol 146 (3) ◽  
pp. 527-534 ◽  
Author(s):  
K H Liu ◽  
J C Huang ◽  
J D Godkin
Keyword(s):  
Protein Production ◽  
Culture Medium ◽  
De Novo ◽  
Binding Protein ◽  
Yolk Sac ◽  
Retinol Binding Protein ◽  
Minimum Essential Medium ◽  
Placental Membranes ◽  
Extraembryonic Membranes

Abstract Caprine chorion, allantois and amnion from days 23, 28, 35, 39 and 45, and yolk sac from day 23 of pregnancy were isolated by dissection and cultured for 24 h in modified minimum essential medium in the presence of [35S] methionine. De novo-synthesized proteins released into the culture medium were analyzed by two-dimensional PAGE and fluorography. Patterns of protein production by these isolated extraembryonic membranes remained relatively unchanged from days 23 to 45 of pregnancy. Electrophoretic profiles of proteins synthesized by allantois and amnion were identical but distinct from that produced by chorion. Yolk sac was the major source of serum-like proteins. An acidic (pI 5·3–6·3) 22 kDa protein, which consisted of four isoelectric variants, was produced by all extraembryonic membranes and demonstrated to immunoreact with antiserum produced against bovine placental retinol-binding protein (RBP). Limited N-terminal sequence analysis of one major isoform indicated that the protein had complete homology with bovine RBP over the first 15 amino acids. Immunoreactive RBP was localized in epithelial cells lining the chorion, allantois and amnion. In this study, we have characterized and compared protein production by isolated extraembryonic membranes through days 23 to 45 of pregnancy and identified the 22 kDa protein as caprine RBP of placental origin. Journal of Endocrinology (1995) 146, 527–534

Cloning and Characterization of Chicken CRBP2 Gene and Comparison with other Vertebrates

2011 ◽  
Vol 343-344 ◽  
pp. 678-682
Author(s):  
Li Hua Xiao ◽  
Fan Li Kong ◽  
Hua Dong Yin ◽  
Xiao Ling Zhao ◽  
Qing Zhu
Keyword(s):  
Vitamin A ◽  
Egg Production ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Production Traits ◽  
Coding Region ◽  
Small Intestinal ◽  
Small Intestinal Villus ◽  
Molecular Nature

Cellular retinol-binding protein 2 (CRBP2), a vitamin A binding protein expressed specifically in small intestinal villus absorptive cells, plays a pivotal role in the intestinal vitamin A absorption, transport, and metabolism pathways. In this study, we cloned the entire coding region of chicken CRBP2 gene. The amplified fragment contains entire coding region sequence with 408 nucleotides, which putatively codes 135 AA. By comparing nine vertebrates, the homology of nucleotide sequences is from 52.3% to 99.8%, while the similarity of AA sequence ranged from 72.4% to 99.3%. Results showed that the CRBP2 gene was conservative among different animal species. This work constructed the basis for further research on the molecular nature and genetic markers of CRBP2 for improving egg production traits in chicken.

scholarly journals Isolation and characterization of isoforms of retinol binding protein by isoelectrofocusing

IUBMB Life ◽  
1997 ◽  
Vol 41 (5) ◽  
pp. 1057-1066
Author(s):  
Zoran Minic ◽  
Jovan Hranisavljevic ◽  
Dusan Vucelic
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Isolation And Characterization
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