PMID- 33143610
OWN - NLM
STAT- MEDLINE
DCOM- 20210701
LR  - 20210701
IS  - 1875-5305 (Electronic)
IS  - 0929-8665 (Linking)
VI  - 28
IP  - 5
DP  - 2021
TI  - A Novel Reversibly Glycosylated Polypeptide-2 of Bee Pollen from Rape (Brassica 
      napus L.): Purification and Characterization.
PG  - 543-553
LID - 10.2174/0929866527666201103161302 [doi]
AB  - BACKGROUND: Reversibly glycosylated polypeptide (RGP), a kind of hydrosoluble and 
      plasmodesmal-associated protein found in plants, plays a crucial role in the 
      development of pollen. OBJECTIVE: A novel RGP 2 was isolated and identified from 
      rape (Brassica napus L.) bee pollen. METHODS: RGP2 was isolated and purified by 
      ion-exchange column and gel filtration chromatography, and characterized by 
      MALDI-TOF-MS, LC-MS, immunological histological chemistry, and transmission 
      electron microscope. RESULTS: Our results indicated that the RGP2 is an acidic 
      protein (pI=5.46) with the molecular weight 42388 Da. It contained 17 kinds of 
      amino acids, among which aspartic acid had the highest amount (71.56 mg/g). 
      Homologous alignment of amino acid sequence results showed that RGP2 was 80.33%, 
      85.02%, 86.06%, and 88.93% identical to Arabidopsis thaliana RGP2 (AtRGP2), Oryza 
      sativa RGP (OsRGP), Triticum aestivum RGP (TaRGP), and Zea maize RGP (ZmRGP), 
      respectively. The localization results showed that RGP2 in rape anther existed in 
      exine and intine of anther cells of rape flower by immunological histological 
      chemistry and the subcellular localization identified that RGP2 appeared around 
      the Golgi apparatus in cytoplasm by transmission electron microscope. CONCLUSION: 
      RGP2 has a highly conserved sequence of amino acid residues and potential 
      glycosylation sites.
CI  - Copyright(c) Bentham Science Publishers; For any queries, please email at 
      epub@benthamscience.net.
FAU - Zhang, Qi
AU  - Zhang Q
AD  - College of Food Science and Engineering, Northwest University, Xi'an, China.
FAU - Sun, Tian
AU  - Sun T
AD  - College of Food Science and Engineering, Northwest University, Xi'an, China.
FAU - Tuo, Xingxia
AU  - Tuo X
AD  - College of Public Health, School of Medicine, Xi'an Jiaotong University, Xi'an, 
      China.
FAU - Li, Yujin
AU  - Li Y
AD  - College of Food Science and Engineering, Ocean University of China, Qingdao, 
      China.
FAU - Yang, Haixia
AU  - Yang H
AD  - College of Public Health, School of Medicine, Xi'an Jiaotong University, Xi'an, 
      China.
FAU - Deng, Jianjun
AU  - Deng J
AD  - School of Chemical Engineering, Northwest University, Xi'an, China.
LA  - eng
GR  - 21978229, 21676212/National Natural Science Foundation of China/
GR  - 2019NY-140/Key Research and Development Program of Shaanxi/
GR  - 2017BSHTDZZ14/Shaanxi Postdoctoral Science Foundation/
PT  - Journal Article
PL  - Netherlands
TA  - Protein Pept Lett
JT  - Protein and peptide letters
JID - 9441434
RN  - 0 (Plant Proteins)
RN  - EC 2.4.1.- (Glucosyltransferases)
SB  - IM
MH  - Animals
MH  - Bees
MH  - Brassica napus/*chemistry/genetics
MH  - Glucosyltransferases/*chemistry/genetics
MH  - Glycosylation
MH  - Plant Proteins/*chemistry/genetics
MH  - Pollen/*chemistry/genetics
OTO - NOTNLM
OT  - MALDI-TOF-MS
OT  - Reversibly glycosylated polypeptide
OT  - Transmission Electron Microscope
OT  - immunological histological chemistry
OT  - peptide mass fingerprinting
OT  - rape bee pollen
EDAT- 2020/11/05 06:00
MHDA- 2021/07/02 06:00
CRDT- 2020/11/04 05:30
PHST- 2020/05/15 00:00 [received]
PHST- 2020/09/15 00:00 [revised]
PHST- 2020/09/15 00:00 [accepted]
PHST- 2020/11/05 06:00 [pubmed]
PHST- 2021/07/02 06:00 [medline]
PHST- 2020/11/04 05:30 [entrez]
AID - PPL-EPUB-111152 [pii]
AID - 10.2174/0929866527666201103161302 [doi]
PST - ppublish
SO  - Protein Pept Lett. 2021;28(5):543-553. doi: 10.2174/0929866527666201103161302.