ChemicalBook CAS DataBase List 9008-02-0

9008-02-0

Name	HEMOGLOBIN
CAS	9008-02-0
EINECS(EC#)	293-254-9
Molecular Formula	NULL
MDL Number	MFCD00131282
Molecular Weight	226.231
MOL File	9008-02-0.mol

Chemical Properties

Definition	The respiratory protein of the red blood cells, it transfers oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its affinity for carbon monoxide is >200 times that for oxygen. Hemoglobin is a conjugated protein of molec
storage temp.	2-8°C
solubility	0.6 M HCl: soluble20mg/mL
form	substrate powder
color	Dark brown powder
biological source	Porcine
Water Solubility	Soluble in water.
Cosmetics Ingredients Functions	SKIN CONDITIONING
InChI	InChI=1S/C13H10N2O2/c1-8-4-5-9-11(16)7-10(15-13(9)14-8)12-3-2-6-17-12/h2-7H,1H3,(H,14,15,16)
InChIKey	INGWEZCOABYORO-UHFFFAOYSA-N
SMILES	N1C2=C(C=CC(C)=N2)C(=O)C=C1C1=CC=CO1
Uses	Medicine, usually called hemoglobin. less more
EPA Substance Registry System	Hemoglobins(9008-02-0)

Safety Data

Hazard Codes	B
Safety Statements	22-24/25 less more
WGK Germany	3
F	1-10
TSCA	Yes
HS Code	3002905150
Storage Class	11 - Combustible Solids

Raw materials And Preparation Products

Hazard Information

Description

Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chains contains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operate independently. The release (and binding) of oxygen is a cooperative process, which means that the loss (uptake) of the first oxygen molecule triggers the release of the remaining three.
The current model for oxygen binding in haemoglobin and myoglobin can be explained in the following way. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane with its four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue. Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe³⁺ centre and O₂ is reduced to [O₂]^-. Both species contain an unpaired electron. The low-spin Fe³⁺ moves into the plane and pulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygen in the other three haeme groups.

General Description

Native hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen.

Biochem/physiol Actions

The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues.

Purification Methods

Purify it from blood using CM-32 cellulose column chromatography. [Matsukawa et al. J Am Chem Soc 107 1108 1985.] For the purification of the and chains see Hill et al. Biochemical Preparations 10 55 1963. Histones (from S4A mouse lymphoma). The purification of histones uses a macroprocess column, heptafluorobutyric acid as solubilising and ion-pairing agent and an acetonitrile gradient. [McCroskey et al. Anal Biochem 163 427 1987.]

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