ピーナッツ凝集素、ピーナッツアグルチニン
WordNet
- widely cultivated American plant cultivated in tropical and warm regions; showy yellow flowers on stalks that bend over to the soil so that seed pods ripen underground (同)peanut vine, Arachis_hypogaea
- underground pod of the peanut vine
- pod of the peanut vine containing usually 2 nuts or seeds; `groundnut and `monkey nut are British terms (同)earthnut, goober, goober pea, groundnut, monkey_nut
- a young child who is small for his age
- an antibody that causes agglutination of a specific antigen
- an insignificant sum of money; a trifling amount; "her salary is peanuts compared to his"
PrepTutorEJDIC
- 『落花生』,南京(なんきん)豆,ピーナッツ(《英》groundnut) / (1年草の)落花生;ピーナッツのさや / 《複数形で》《米俗》つまらない絹(物);ごく少額の金
- 凝集素(赤血球などの凝集反応を起こす抗体)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/01 21:17:10」(JST)
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Peanut Agglutinin complexed with a di-galactose. PDB entry 2dvd
Peanut agglutinin (PNA) is plant lectin protein derived from the fruits of Arachis hypogaea. Peanut agglutinin may also be referred to as Arachis hypogaea lectin. Lectins recognise and bind particular sugar sequences in carbohydrates; peanut agglutinin binds the carbohydrate sequence Gal-β(1-3)-GalNAc. The name "peanut agglutinin" originates from its ability to stick together (agglutinate) cells, such as neuramidase-treated erythrocytes,[1] which have glycoproteins or glycolipids on their surface which include the Gal-β(1-3)-GalNAc carbohydrate sequence.
Contents
- 1 Structure
- 2 Uses in cell biology and biochemistry
- 3 See also
- 4 References
Structure
| Legume lectin domain |
|
Structure of the monosaccharide binding site of lentil lectin.[2]
|
| Identifiers |
| Symbol |
Lectin_legB |
| Pfam |
PF00139 |
| Pfam clan |
CL0004 |
| InterPro |
IPR001220 |
| PROSITE |
PDOC00278 |
| SCOP |
1lem |
| SUPERFAMILY |
1lem |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
The protein is 273 amino acids in length with the first 23 residues acting and a signal peptide which is subsequently cleaved. It has a Uniprot accession of P02872. There are over 20 structures of this protein in the PDB which reveal and all beta-sheet protein with a tetrameric quaternary structure. It is a member of the Lectin_legB PFAM family.
Available Structures of peanut agglutinin
Uses in cell biology and biochemistry
Because peanut agglutinin specifically binds a particular carbohydrate sequence it finds use in a range of methods for cell biology and biochemistry. For example in PNA-affinity chromatography the binding specificity of peanut agglutinin is used to isolate glycosylated molecules which have the sugar sequence Gal-β(1-3)-GalNAc. Peanut agglutinin activity is inhibited by lactose and galactose which compete for the binding site.
Other uses include:
- Potent anti-T cell activity.
- Distinguishing between human lymphocyte subsets.
- Tumour tissue determination for transitional mucosa malignancies.
- Identification of mammalian-infective metacyclic promastigote Leishmania major parasites from other life cycle forms also found in the sandfly host.
- Identification of the outer acrosome membrane in sperm, indicating acrosome integrity. [3]
See also
- List of histologic stains that aid in diagnosis of cutaneous conditions
References
- ^ "PNA specification sheet Medicago AB:" (PDF). Retrieved 2010 Mars 14.
- ^ Loris R, Casset F, Bouckaert J, et al. (December 1994). "The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study". Glycoconj. J. 11 (6): 507–17. doi:10.1007/bf00731301. PMID 7696853.
- ^ Blumer, Camile Garcia; Restelli, Adriana Ester; Giudice, Paula Toni Del; Soler, Thiesa Butterby; Fraietta, Renato; Nichi, Marcilio; Bertolla, Ricardo Pimenta; Cedenho, Agnaldo Pereira. "Effect of varicocele on sperm function and semen oxidative stress". BJU International 109 (2): 259–265. doi:10.1111/j.1464-410X.2011.10240.x.
UpToDate Contents
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English Journal
- Design and synthesis of hydrolytically stable multivalent ligands bearing thiodigalactoside analogues for peanut lectin and human galectin-3 binding.
- Cagnoni AJ, Kovensky J, Uhrig ML.
- The Journal of organic chemistry.J Org Chem.2014 Jun 17. [Epub ahead of print]
- Herein, we describe the design and synthesis of a novel family of hydrolytically stable glycoclusters bearing thiodigalactoside (TDG) analogues as recognition elements of beta-galactoside binding lectins. The TDG analogue was synthesized by thioglycosylation of a 6-S-acetyl-alpha-D-glucosyl bromide
- PMID 24937526
- Lectin-decorated nanoparticles enhance binding to the inflamed tissue in experimental colitis.
- Moulari B1, Beduneau A1, Pellequer Y1, Lamprecht A2.
- Journal of controlled release : official journal of the Controlled Release Society.J Control Release.2014 Jun 6. pii: S0168-3659(14)00349-6. doi: 10.1016/j.jconrel.2014.05.046. [Epub ahead of print]
- A major limitation in the drug treatment of inflammatory bowel disease is the inability to deliver the drug selectively towards the inflamed tissues. Nanotechnology-based drug delivery systems have led to an amelioration of the therapeutic selectivity but still the majority of the entrapped drug is
- PMID 24910194
- Characterization of the Proliferating Cell Nuclear Antigen of Leishmania donovani Clinical Isolates and Its Association with Antimony Resistance.
- Tandon R1, Chandra S2, Baharia RK1, Das S1, Misra P1, Kumar A1, Siddiqi MI2, Sundar S3, Dube A4.
- Antimicrobial agents and chemotherapy.Antimicrob Agents Chemother.2014 Jun;58(6):2997-3007. Epub 2014 Mar 10.
- Previously, through a proteomic analysis, proliferating cell nuclear antigen (PCNA) was found to be overexpressed in the sodium antimony gluconate (SAG)-resistant clinical isolate compared to that in the SAG-sensitive clinical isolate of Leishmania donovani. The present study was designed to explore
- PMID 24614385
Japanese Journal
- Simultaneous evaluation of plasma membrane integrity, acrosomal integrity, and mitochondrial membrane potential in bovine spermatozoa by flow cytometry
- Effects of acrosomal conditions of frozen-thawed spermatozoa on the results of artificial insemination in Japanese Black cattle
- Effects of acrosomal conditions of frozen-thawed spermatozoa on the results of artificial insemination in Japanese Black cattle
Related Links
- Peanut agglutinin (PNA) is plant lectin protein derived from the fruits of Arachis hypogaea. Peanut agglutinin may also be referred to as Arachis hypogaea lectin. Lectins recognise and bind particular sugar sequences in carbohydrates; peanut ...
- Peanut agglutinin binds preferentially to the T-antigen, a galactosyl N- acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated ...
★リンクテーブル★
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- 英
- peanut agglutinin
- 関
- ピーナッツアグルチニン
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- 英
- peanut agglutinin
- 関
- ピーナッツ凝集素
[★]
ピーナッツ
- 関
- Arachis、Arachis hypogaea
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