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Structural Studies of Human Hemopexin
1984Abstract The primary structure of human hemopexin (Hpx) is being deduced from sequence analysis of a series of peptides obtained from chemical and enzymatic digests of the protein. Human Hpx consists of about 440 amino acid residues. It has five sites of attachment of GlcN oligosaccharides at the signal sequence of Asn-X-Thr/Ser.
NOBUHIRO TAKAHASHI +2 more
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Genetic control of serum hemopexin.
Annals of clinical research, 1977Serum hemopexin was studied in a sample of twin pairs. Among monozygotic twin pairs a high concordance was found for serum hemopexin. This zygosity group analysis of variance also showed a significantly lower variance within than between pairs. The results indicate that the concentration of serum hemopexin is strongly influenced by genetic factors.
M, Myrhed +2 more
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Hemopexin and haptoglobin: allies against heme toxicity from hemoglobin not contenders
Frontiers in Physiology, 2015Ann Smith, Russell J Mcculloh
exaly

