Determination of royal jelly freshness by ELISA with a highly specific anti-apalbumin 1, major royal jelly protein 1 antibody*
| Autor: | Wen-xiu Zhou, Tan Liangliang, Mei-lu Li, Wang Yiran, Dan-dan Liu, Lirong Shen, Fa Xiao, Liang Zhai |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
food.ingredient
Bioinformatics analysis Enzyme-Linked Immunosorbent Assay General Biochemistry Genetics and Molecular Biology Antibodies law.invention food Western blot law Royal jelly Materials Testing medicine General Pharmacology Toxicology and Pharmaceutics Glycoproteins Gel electrophoresis chemistry.chemical_classification General Veterinary biology medicine.diagnostic_test Fatty Acids General Medicine Articles Molecular biology chemistry Polyclonal antibodies Recombinant DNA biology.protein Insect Proteins Antibody Glycoprotein |
| Popis: | Major royal jelly protein 1 (MRJP1), designated apalbumin 1, has been regarded as a freshness marker of royal jelly (RJ). A MRJP1-specific peptide (IKEALPHVPIFD) identified by bioinformatics analysis of homologous members of the major royal protein family was synthesized and used to raise polyclonal anti-MRJP1 antibody (anti-SP-MRJP1 antibody). Western blot analysis showed that anti-SP-MRJP1 antibody only reacted with MRJP1 in RJ. In contrast, the previously reported antibody against recombinant MRJP1 (anti-R-MRJP1 antibody) reacted with other members of MRJP family in RJ. Enzyme-linked immunosorbent assay (ELISA) using anti-SP-MRJP1 antibody demonstrated that MRJP1 content in RJ stored at 40 °C significantly degraded by 37.3%, 55.9%, 58.0%, 60.6%, 65.7%, 72.7%, and 73.1% at 7, 14, 21, 28, 35, 42, and 49 d, respectively, when compared with MRJP1 content in fresh RJ (0 d). Optical density analysis of MRJP bands from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles demonstrated that the degradation of MRJP1, MRJP2, MRJP3, and MRJP5 in RJ was strongly and positively correlated with the period of storage (P |
| Databáze: | OpenAIRE |
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