Logo: to the web site of Uppsala University

uu.sePublikasjoner fra Uppsala universitet
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Calliandra selloi Macbride trypsin inhibitor: isolation, characterization, stability, spectroscopic analyses
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwiginstitutet för cancerforskning.
Vise andre og tillknytning
2007 (engelsk)Inngår i: Phytochemistry, ISSN 0031-9422, E-ISSN 1873-3700, Vol. 68, nr 21, s. 2625-2634Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

A trypsin inhibitor was purified from Calliandra selloi Macbride seeds (CSTI). SDS-PAGE under non-reducing conditions showed a single band of approximately 20,000Da, while under reducing conditions two bands of 16,000 and 6000Da were observed, indicating that CSTI consists of two polypeptide chains. Molecular masses of 20,078 and 20,279 were obtained by mass spectrometry, although only one pI of 4.0 was observed and one peak was obtained by reversed phase chromatography. Amino-terminal sequence analysis showed homology to Kunitz-type inhibitors. CSTI was able to inhibit trypsin (K(i) 2.21x10(-7)M), alpha-chymotrypsin (K(i) 4.95x10(-7)M) and kallikrein (K(i) 4.20x10(-7)M) but had no effect on elastase. Trypsin inhibitory activity was stable over a wide range of pH and temperature. CSTI was particularly susceptible to DTT treatment, followed by addition of iodoacetamide. Far-UV circular dichroism measurements revealed that CSTI is a beta-II protein. Thermal unfolding showed a two-state transition with a midpoint at 68 degrees C. Far-UV CD spectra of CSTI at pH extremes showed little changes, while more pronounced differences in near-UV CD spectra were detected. Remarkably, treatment with 1mM DTT caused very slight changes in the far-UV CD spectrum, and only after carbamidomethylation was there was a marked loss observed in secondary structure.

sted, utgiver, år, opplag, sider
2007. Vol. 68, nr 21, s. 2625-2634
Emneord [en]
Calliandra selloi MacBride, Characterization, Kunitz-type trypsin inhibitor, Leguminosae, Protein purification, Stability studies
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-11978DOI: 10.1016/j.phytochem.2007.06.003ISI: 000255536700003PubMedID: 17651769OAI: oai:DiVA.org:uu-11978DiVA, id: diva2:39747
Tilgjengelig fra: 2007-11-08 Laget: 2007-11-08 Sist oppdatert: 2017-12-11bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMed

Person

Hellman, Ulf

Søk i DiVA

Av forfatter/redaktør
Hellman, Ulf
Av organisasjonen
I samme tidsskrift
Phytochemistry

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 451 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf