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Related Concept Videos

Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

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Related Experiment Video

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A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging
09:37

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Published on: July 14, 2016

Haptocorrin in humans.

Anne L Morkbak1, Steen S Poulsen, Ebba Nexo

  • 1Department of Clinical Biochemistry, Aarhus University Hospital, Aarhus, Denmark.

Clinical Chemistry and Laboratory Medicine
|November 10, 2007
PubMed
Summary

Haptocorrin, a vitamin B12-binding protein, is found in many tissues, including fetal tissues. In vitamin B12 deficiency, analogues accumulate on haptocorrin, suggesting a role in monitoring B12 status.

Area of Science:

  • Biochemistry
  • Human Physiology
  • Evolutionary Biology

Background:

  • Haptocorrin (also known as R-binder) is the most recently evolved cobalamin-binding protein, originating from the intrinsic factor gene.
  • Its function and distribution in fetal and adult life are not fully understood, despite its known ability to bind cobalamin and analogues.

Purpose of the Study:

  • To investigate the tissue expression of haptocorrin in humans.
  • To explore the relationship between haptocorrin-bound analogues and vitamin B12 status.

Main Methods:

  • Immunohistochemistry was used to determine haptocorrin localization in fetal and adult tissues.
  • Enzyme-linked immunosorbent assay (ELISA) measured holo- and total haptocorrin in blood samples from individuals with varying vitamin B12 deficiency levels, confirmed by methylmalonic acid measurements.

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Main Results:

  • Haptocorrin was found in various exocrine glands, the gastrointestinal tract, and the respiratory system.
  • Individuals with vitamin B12 deficiency exhibited significantly higher levels of haptocorrin-bound analogues compared to non-deficient individuals.

Conclusions:

  • Haptocorrin is widely distributed, including in fetal tissues.
  • The accumulation of analogues on haptocorrin in vitamin B12 deficiency suggests its potential as a biomarker, warranting further investigation.