Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydrolysate.
about
The multiple functions of hemoglobinControlled Enzymatic Hydrolysis: A New Strategy for the Discovery of Antimicrobial Peptides.Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins.Organic solvent extraction associated with HPLC in the preparation of hemorphins from bovine hemoglobin peptic hydrolysate.SwePep, a database designed for endogenous peptides and mass spectrometry.Hemoglobin-derived peptides as novel type of bioactive signaling moleculesNovel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme.Bioactive angiotensin peptides: focus on angiotensin IV.Food proteins as a source of bioactive peptides with diverse functions.Identification and functional characterization of hemorphins VV-H-7 and LVV-H-7 as low-affinity agonists for the orphan bombesin receptor subtype 3.A globin fragment, LVV-hemorphin-7, induces [3H]thymidine incorporation in a neuronal cell line via the AT4 receptor.Primary structure and biological activity of hemoglobin-related hypothalamic peptides.Peptic hemoglobin hydrolysis in an ultrafiltration reactor at pilot plant scale generates opioid peptides.In vivo processing of LVV-hemorphin-7 in rat brain and blood utilizing microdialysis combined with electrospray mass spectrometry.Influence of pH on the appearance of active peptides in the course of peptic hydrolysis of bovine haemoglobin.High molecular weight aspartic endopeptidase generates a coronaro-constrictory peptide from the beta-chain of hemoglobin.Peptides: Production, bioactivity, functionality, and applications.LVV- and VV-hemorphins: comparative levels in rat tissues.Generation of VV-hemorphin-7 from globin by peritoneal macrophagesA Rapid Detection and Identification of Hemorphins Released from Bovine Hemoglobin Enzymatic Hydrolysis by Use of HPLC Coupled with Photodiode Array DetectorSlaughterhouse Blood: An Emerging Source of Bioactive Compounds
P2860
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P2860
Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydrolysate.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@en
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@nl
type
label
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@en
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@nl
prefLabel
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@en
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@nl
P2093
P1476
Isolation and characterization ...... hemoglobin peptic hydrolysate.
@en
P2093
P304
P356
10.1016/0006-291X(92)91531-T
P407
P577
1992-11-01T00:00:00Z