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1.
Genet Mol Res ; 15(3)2016 Aug 12.
Article in English | MEDLINE | ID: mdl-27525943

ABSTRACT

The amino acids in royal jelly (RJ) have a wide range of pharmacological and health-promoting functions in humans. Multiple studies on the amino acid quality and composition in RJ have investigated RJ harvested at 72 h after larval transfer. In contrast, the concentration of amino acids in RJ harvested before 72 h remains unknown. In this study, the concentration of free amino acids (FAAs) and total amino acids (TAAs) in RJ harvested at 13 time points between 24 and 72 h after transfer of ten Apis mellifera colonies were measured. Our results indicated that the most abundant FAAs were Pro, Phe, Lys, Glu, and Tyr, whereas the most abundant TAAs were Asp, Glu, Leu, Lys, and Val. The total FAA concentration in RJ increased with increasing harvest time, from 4.30 mg/g at 24 h to 9.48 mg/g at 72 h. In contrast, the variation in concentration of TAAs observed was a decrease-increase-decrease trend with 40 h (149.53 mg/g) and 52 h (169.62 mg/g) as inflection points. The highest and lowest concentrations of TAA were 197.96 and 121.32 mg/g at 24 and 72 h, respectively. To our knowledge, this is the first study to investigate the concentration changes of FAAs and TAAs prior to 72 h after transfer. Our results will provide theoretical support to guide production practices of beekeeping, as well as elucidate the relationship between the harvest time point and RJ content.


Subject(s)
Amino Acids/chemistry , Fatty Acids/chemistry , Animal Husbandry , Animals , Bees/physiology , Larva/physiology , Time Factors
2.
Genet Mol Res ; 14(4): 16185-95, 2015 Dec 08.
Article in English | MEDLINE | ID: mdl-26662411

ABSTRACT

Sensing bitter tastes is crucial for most animals because it can prevent them from ingesting harmful food. This process is mainly mediated by the bitter taste receptors (T2R) that are largely expressed in the taste buds. Previous studies have identified some T2R gene repertoires. Marked variation in repertoire size has been noted among species. However, research on T2Rs is still limited and the mechanisms underlying the evolution of vertebrate T2Rs remain poorly understood. In the present study, we analyzed the structure and features of the protein encoded by the forest musk deer (Moschus berezovskii) T2R16 and submitted the gene sequence to NCBI GenBank. The results showed that the full coding DNA sequence (CDS) of musk deer T2R16 (GenBank accession No. KP677279) was 906 bp, encoding 301 amino acids, which contained ATG start codon and TGA stop codon, with a calculated molecular weight of 35.03 kDa and an isoelectric point of 9.56. The T2R16 protein receptor had seven conserved transmembrane regions. Hydrophobicity analysis showed that most amino acid residues in T2R16 protein were hydrophobic, and the grand average of hydrophobicity (GRAVY) was 0.657. Phylogenetic analysis based on this gene revealed that forest musk deer had the closest association with sheep (Ovis aries), as compared to cow (Bos taurus), Tursiops truncatus, and other species, whereas it was genetically farthest from humans (Homo sapiens). We hope these results would complement the existing data on T2R16 and encourage further research in this respect.


Subject(s)
Cloning, Molecular , Deer/genetics , Evolution, Molecular , Receptors, G-Protein-Coupled/genetics , Animals , Deer/classification , Deer/metabolism , Hydrophobic and Hydrophilic Interactions , Phosphorylation , Phylogeny , Protein Interaction Domains and Motifs , Receptors, G-Protein-Coupled/chemistry , Receptors, G-Protein-Coupled/metabolism , Sequence Analysis, DNA
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