In vitro molecular structure of N-terminal B-type natriuretic peptide: Monomer or oligomer?

Clinical Chemistry

Volumn 57, Issue 6, 2011, Pages 924-926

  Crimmins, Dan L ^a   Goetze, Jens Peter ^b  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL PRO BRAIN NATRIURETIC PEPTIDE; ANTIBODY; MONOMER; OLIGOMER;

DEGLYCOSYLATION; ELUTION; GEL FILTRATION; HEART FAILURE; HUMAN; IMMUNOASSAY; IMMUNOREACTIVITY; IN VITRO STUDY; LETTER; OLIGOMERIZATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; WESTERN BLOTTING;

ANIMALS; HUMANS; IMMUNOASSAY; NATRIURETIC PEPTIDE, BRAIN; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RATS; RECOMBINANT PROTEINS;

EID: 79957749052     PISSN: 00099147     EISSN: 15308561     Source Type: Journal    
DOI: 10.1373/clinchem.2010.160259     Document Type: Letter

References (5)

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2. Ala-Kopsala M, Moilanen A-M, Rysä J, Ruskoaho H, Vuolteenaho O. Characterization of molecular forms of N-terminal B-type natriuretic peptide in vitro. Clin Chem 2010;56:1822-9.
3. Becker GW, Bowsher RR, Mackellar WC, Poor ML, Tackitt PM, Riggin RM. Chemical, physical, and biological characterization of a dimeric form of biosynthetic human growth hormone. Biotechnol Appl Biochem 1987;9:478-87. (Pubitemid 18016727)
4. Crimmins DL. Human N-terminal proBNP is a monomer. Clin Chem 2005;51:1035-8. (Pubitemid 40740891)
5. Crimmins DL, Kao JL. The human cardiac hormone fragment N-terminal pro B-type natriuretic peptide is an intrinsically unstructured protein. Arch Biochem Biophys 2007;461:242-6. (Pubitemid 46677891)