کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5133054 | 1492051 | 2018 | 9 صفحه PDF | دانلود رایگان |
- A 75Â kDa red colour-related protein (LvPBP75) was purified from the shell of Litopenaeus vannamei.
- LvPBP75 was identified as hemocyanin by MALDI-TOF-MS and cDNA cloning.
- LvPBP75 cDNA contains a 1986Â bp ORF, that encodes a protein of 662 amino acids.
- Novel function of hemocyanin as binding with pigment, and correlated with shrimp shell colour change.
Pigment-binding proteins play important roles in crustacean shell colour change. In this study, a red colour-related pigment-binding protein, designated LvPBP75, was purified from the shell of Litopenaeus vannamei. HPLC and PAGE analysis showed that LvPBP75 was a homogeneous monomer with molecular mass of 75 kDa. Peptide mass fingerprint analysis revealed that LvPBP75 belonged to hemocyanin, and the released pigment from heated LvPBP75 showed a λmax at 481 nm in acetone. The significant red-colour change temperatures were detected at 30 and 80 °C, respectively. Based on the determined amino acid fragments, a full-length cDNA of LvPBP75 was cloned and sequenced. The ORF encodes a protein of 662 amino acids having 80% identity with penaeidae hemocyanin. These results strongly suggest a novel function of hemocyanin, namely binding with pigment, and its involvement in L. vannamei shell colour change.
Journal: Food Chemistry - Volume 241, 15 February 2018, Pages 104-112