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Posttranslational modification / Protein domains / Protein structure / Trypsin / Phosphorylation / Testin / Secretion / Biology / Cell biology / Peptidase


Molecular Membrane Biology, October /December 2003, 20, 307 /317 Structural and functional characterization of the human NBC3 sodium/ bicarbonate co-transporter carboxyl-terminal cytoplasmic domain Frederick B. Loisel
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Document Date: 2011-01-07 15:42:11


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City

Edmonton / Bradford / L.A. / /

Company

Kodak / IgG / NBC3Ct Limited / BT / Life Technologies Inc. / NBC / Millipore / Ethyl / Racusen L. C. / Becton Dickinson / Taylor & Francis Ltd / Pharmacia / /

Country

Canada / /

Currency

pence / /

/

Facility

Stanford University / Alberta Peptide Institute / University of Alberta / /

IndustryTerm

serum-free media / cell surface processing / optimization protocol / analysis software / bacterial protein product / cleavage site / phosphorylation site / restriction site / surface processing / cystic fibrosis gene product / poor processing / analysed using JASCO J700 analysis software / /

MedicalCondition

transient alkalosis / acidosis / cystic fibrosis / maximum acidosis / /

NaturalFeature

Cl channel / /

Organization

University of Alberta / Department of Physiology / Alberta Heritage Foundation for Medical Research / Department of Biochemistry / Stanford University / Alberta Peptide Institute / Natural Sciences and Engineering Research Council / New York Academy of Science / /

Person

Alvarez / Ira Kurtz / Sterling / Joseph R. Casey / Frederick B. Loiselle / Paul Jaschke / /

Position

Teller / Representative / /

Product

sodium bicarbonate / acetic acid / glycine / /

SportsLeague

Stanford University / /

Technology

electrophoresis / same optimization protocol / cloning / laser / spectroscopy / /

URL

http /

SocialTag