Dr. Anna E Eckhardt MD
OB-GYN (Obstetrician-Gynecologist)
700 Ne 87th Ave Vancouver WA, 98664Rating
5/5
About
Dr. Anna Eckhardt is an obstetrician-gynecologist practicing in Vancouver, WA. Dr. Eckhardt specializes in women's health, particularly the female reproductive system, pregnancy and childbirth. As an obstetrician-gynecologist, or OB-GYN, Dr. Eckhardt can treat a number of health issues related to the vagina, uterus, ovaries, fallopian tubes and breasts. Dr Eckhardt can also treat women during pregnancy, labor, childbirth and the postpartum period. In this specialty, doctors focus on reproductive care from puberty through adulthood.
Board Certification
Obstetrics and GynecologyAmerican Board of Obstetrics and GynecologyABOG
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase specific for glycosylation of threonine residues.
- Electrochemical sensor for detection of unmodified nucleic acids.
- Automated electrotransformation of on a digital microfluidic platform using bioactivated magnetic beads.
- The subcellular localization of apomucin and nonreducing terminal N-acetylgalactosamine in porcine submaxillary glands.
- The distribution and localization of the fucose-binding lectin in rat tissues and the identification of a high affinity form of the mannose/N-acetylglucosamine-binding lectin in rat liver.
- The nonidentity of porcine N-acetylglucosaminyltransferases I and II.
- The preparation of UDP-N-acetylgalactosamine from UDP-N-acetylglucosamine employing UDP-N-acetylglucosamine-4-epimerase.
- [Pregnancy, labor and early neonatal period characteristics according to legitimacy].
- Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland.
- The acceptor substrate specificity of porcine submaxillary UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is dependent on the amino acid sequences adjacent to serine and threonine residues.
- Porcine submaxillary mucin forms disulfide-bonded dimers between its carboxyl-terminal domains.
- Probing biomolecule recognition with electron transfer: electrochemical sensors
- The complete cDNA sequence and structural polymorphism of the polypeptide chain
- Porcine submaxillary mucin forms disulfide-linked multimers through its amino-terminal D-domains.
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Practice At 700 Ne 87th Ave
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