scholarly journals Purification and characterization of a uterine retinol-binding protein in the bitch

1995 ◽  
Vol 311 (2) ◽  
pp. 407-415 ◽  
Author(s):  
W C Buhi ◽  
I M Alvarez ◽  
V M Shille ◽  
M J Thatcher ◽  
J P Harney ◽  
...  

A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.

2019 ◽  
Vol 14 (1) ◽  
pp. 31 ◽  
Author(s):  
Asda Laining ◽  
Ike Trismawanti ◽  
Usman Usman ◽  
Muhammad Hafid Masruri

A four months feeding trial was conducted to evaluate the effects of two maturation diets containing either fishmeal (FM) or squid liver meal (SLM) as the major protein source on growth, gonadosomatic index and gonadal bio-chemical profiles of golden spotted rabbitfish, Siganus guttatus. The two tested diets were formulated to be iso-nitrogenous (40%) and iso-lipidic (14%) and supplemented with several micronutrients specifically for gonadal development. The initial weight of golden spotted rabbitfish used were 352.6 ± 45.0 g and stocked into four of 2 m x 2 m x 2.5 m net cages with 25 fish per cage. The test diets were fed to the stocks twice a day. After four months feeding, the weight gains (WG) of broodstock fed the two diets were nearly similar in which FM had WG of 40.1 ± 2.2% and 42.8 ± 2.0% for SLM. The GSI of male fed SLM diet was similar to that of fed with FM. However, the GSI of female fed FM was 5.6 ± 0.1% significantly lower (P<0.05) than SLM which was 11.4 ± 0.5%. Furthermore, total amino acid (TAA) in spermatocyte was significantly (P<0.05) influenced by dietary SLM indicated by its higher TAA (62.4%) compared to TAA content of FM group (46.1%). Similarly, the TAA content in oocyte was significantly (P<0.05) improved when fed SLM. The dietary SLM did not affect the TAA content in the fillet of rabbitfish demonstrated by the similarity of the fillet TAA content in the two groups which was 55.6% for FM and 54.1% for SLM. Dietary SLM enhanced GSI of female broodstocks and profile of amino acid in the gonad of golden spotted rabbitfish, Siganus guttatus.


1987 ◽  
Vol 92 (2) ◽  
pp. 115-146 ◽  
Author(s):  
Lars Rask ◽  
Helena Anundi ◽  
Jan Fohlman ◽  
Per A. Peterson

2010 ◽  
Vol 43 (3) ◽  
pp. 320-323 ◽  
Author(s):  
Beverly J. Tepper ◽  
Youn-Kyung Kim ◽  
Varsha Shete ◽  
Elena Shabrova ◽  
Loredana Quadro

1991 ◽  
Vol 11 (2) ◽  
pp. 963-971
Author(s):  
B Fenton ◽  
J T Clark ◽  
C M Khan ◽  
J V Robinson ◽  
D Walliker ◽  
...  

Merozoite surface antigen MSA-2 of the human parasite Plasmodium falciparum is being considered for the development of a malaria vaccine. The antigen is polymorphic, and specific monoclonal antibodies differentiate five serological variants of MSA-2 among 25 parasite isolates. The variants are grouped into two major serogroups, A and B. Genes encoding two different variants from serogroup A have been sequenced, and their DNA together with deduced amino acid sequences were compared with sequences encoded by other alleles. The comparison shows that the serological classification reflects differences in DNA sequences and deduced primary structure of MSA-2 variants and serogroups. Thus, the overall homologies of DNA and amino acid sequences are over 95% among variants in the same serogroup. In contrast, similarities between the group A variants and a group B variant are only 70 and 64% for DNA and amino acid sequences, respectively. We propose that the MSA-2 protein is encoded by two highly divergent groups of alleles, with limited additional polymorphism displayed within each group.


2007 ◽  
Vol 86 (5) ◽  
pp. 1310-1315 ◽  
Author(s):  
Jennifer Shea ◽  
Edward Randell ◽  
Sudesh Vasdev ◽  
Peizhong Peter Wang ◽  
Barbara Roebothan ◽  
...  

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