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Article

Molecular heterogeneity and alternative splicing of human lactoperoxidase.

Archives of biochemistry and biophysics - 1 Feb 2009

Fragoso Miryam A, Torbati Aliza, Fregien Nevis, Conner Gregory E

Abstract excerpt

Human lactoperoxidase (LPO) exists as two distinct molecules independent of glycosylation. The N-terminus of one form is blocked and has not been identified while the other is proteolytically processed at the N-terminus similar to myeloperoxidase. Our analysis identified alternatively spliced human LPO mRNAs that may explain the observed molecular heterogeneity of LPO. Two mRNAs omit propeptide encoding exons...

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Identifiers

PMID: 19059195
DOI: 10.1016/j.abb.2008.11.015
PMCID: PMC2760484

Genes

LPO

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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