Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle.

Journal of agricultural and food chemistry - 18 Oct 2006

Grunwald Eric W, Richards Mark P

Abstract excerpt

The hemoglobin variant rHb 0.1, which possesses a decreased ability to form subunits, stimulated lipid oxidation in washed fish muscle less effectively as compared to wild-type hemoglobin (rHb 0.0). This could be due to the lower hemin affinity and more rapid autoxidation rate of subunits as compared to tetramers. To differentiate between hemin affinity and autoxidation effects, ferrous V68T Mb was compared to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Gadus morhua
Share to Hemeproteins
Share to Hemin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemoglobins

Share to Hot Temperature

Share to Lipid Peroxidation

Share to Muscles

Share to Myoglobin

Source

Identifiers

PMID: 17032039
DOI: 10.1021/jf061231d

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle.PMID 17032039Read ↗

Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle.Semantic proximity Read ↗

The mechanism of autooxidation of myoglobin.Semantic proximity Read ↗

Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro.Semantic proximity Read ↗

Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin.Semantic proximity Read ↗

Role of tyrosine-103 in myoglobin peroxidase activity: kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H(2)O(2).Semantic proximity Read ↗

Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: possibly related to the rates of hemin release.Semantic proximity Read ↗

Relative roles of heme-irons and globin-thiols in the genesis of acellular hemoglobin mediated vasoconstriction.Semantic proximity Read ↗

Exploring Oxidative Reactions in Hemoglobin Variants Using Mass Spectrometry: Lessons for Engineering Oxidatively Stable Oxygen Therapeutics.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.