Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/15211
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dc.contributor.authorSithigorngul P.
dc.contributor.authorPanchan N.
dc.contributor.authorChaivisuthangkura P.
dc.contributor.authorLongyant S.
dc.contributor.authorSithigorngul W.
dc.contributor.authorPetsom A.
dc.date.accessioned2021-04-05T04:33:02Z-
dc.date.available2021-04-05T04:33:02Z-
dc.date.issued2002
dc.identifier.issn1969781
dc.identifier.other2-s2.0-0036848248
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0036848248&doi=10.1016%2fS0196-9781%2802%2900180-8&partnerID=40&md5=5586d5508a1bf61ae6d6a931ebb3879f
dc.identifier.urihttp://ir.swu.ac.th/jspui/handle/123456789/15211-
dc.description.abstractMouse antiserum against C-terminal amide of Pem-CMG (a peptide in the family of CHH/MIH/GIH) penta-deca peptide (RPRQRNQYRAALQRLamide=CMG-15) was generated and used for localization of the peptide in tissue and extract of the eyestalk of Penaeus monodon by means of immunohistochemistry and dot-ELISA in comparison with anti-T+ antiserum (T+=YANAVQTVamide: the putative C-terminal amide of crustacean hyperglycemic hormone (CHH) of Macrobrachium rosenbergii). The anti-CMG-15 antiserum did not show cross-reactivity to T+ peptide by dot-ELISA and vice versa for anti-T+ antiserum. In dot-ELISA of eyestalk extract of P. monodon after one step separation by RP-HPLC, anti-CMG-15 antiserum recognized different peptide fractions (F38-39) from those recognized by anti-T+ antiserum (F19, 40-41 and 47-51). Most of the T+ immunoreactive fractions (except F19) show higher hyperglycemic activity than the CMG immunoreactive fractions. In immunohistochemical localization, anti-CMG antiserum recognized only 2-3 neurons in medulla terminalis X-organ complex (MTXO) with long processes terminated in the sinus gland. The CMG-immunoreactive neurons were clearly distinct from CHH containing neurons situated in the same area. This evidence confirms the existing of CMG peptide which may play distinct roles from CHHs in hormonal regulation in P. monodon. © 2002 Elsevier Science Inc. All rights reserved.
dc.subjectantiserum
dc.subjectarginylpropylarginylglutaminylarginylasparaginylglutaminyltyrosylarginylala nylalanylleucylglutaminylarginylleucinamide
dc.subjectpeptide antibody
dc.subjectpolypeptide
dc.subjecttyrosylalanylasparaginylalanylvalylglutaminylthreonylvalinamide
dc.subjectunclassified drug
dc.subjecthyperglycemic hormone, crustacean
dc.subjectnerve protein
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectcross reaction
dc.subjectCrustacea
dc.subjectenzyme linked immunosorbent assay
dc.subjecteye
dc.subjecthormonal regulation
dc.subjectimmunocompetent cell
dc.subjectimmunohistochemistry
dc.subjectimmunoreactivity
dc.subjectnerve cell
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein expression
dc.subjectprotein localization
dc.subjecttiger
dc.subjecttissue distribution
dc.subjectamino acid sequence
dc.subjectanimal
dc.subjectchemistry
dc.subjecteye
dc.subjectimmunology
dc.subjectmetabolism
dc.subjectmolecular genetics
dc.subjectsequence homology
dc.subjectCrustacea
dc.subjectMacrobrachium
dc.subjectMacrobrachium rosenbergii
dc.subjectMonodon
dc.subjectPanthera tigris
dc.subjectPenaeus monodon
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCrustacea
dc.subjectEnzyme-Linked Immunosorbent Assay
dc.subjectEye
dc.subjectImmune Sera
dc.subjectImmunohistochemistry
dc.subjectMolecular Sequence Data
dc.subjectNerve Tissue Proteins
dc.subjectSequence Homology, Amino Acid
dc.titleDifferential expression of CMG peptide and crustacean hyperglycemic hormones (CHHs) in the eyestalk of the giant tiger prawn Penaeus monodon
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationPeptides. Vol 23, No.11 (2002), p.1943-1952
dc.identifier.doi10.1016/S0196-9781(02)00180-8
Appears in Collections:Scopus 1983-2021

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