CAS號9008-02-0 Hemoglobin
貨號：H8020
規(guī)格：5g/瓶

• 別名：Hb 牛血紅蛋白 高鐵血紅蛋白 Hemoglobin

• 英文名稱：Hemoglobin from bovine blood Hemoglobin

• CAS：9008-02-0

• 儲存條件：干燥保存

• 外觀（性狀）：深紅色結(jié)晶性粉末。

• 單位：瓶

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• CAS NUMBER: 9008-02-0
• SYNONYMS: Hb; Ferrohemoglobin
• PHYSICAL PROPERTIES:
• Appearance: Red-brown powder
• pI: 6.8 4
• UV Data: Extinction coefficients of hemoglobin from different species vary due to differences in amino acid
• composition and sequence of the globin chains. 1 Spectral assays of oxyHb, deoxyHb and ferriHb have been
• reported in the literature. 6,7 Extinction coefficients are strongly pH-dependent. 6
• Molecular weight: Mammalian hemoglobins have molecular weights of -64,500. 1
• SOLUBILITY / SOLUTION STABILITY:
• Hemoglobin is soluble in water (1 part in 7 of water), and slowly soluble in glycerol. 1 tests the
• solubility in water or in 100 mM phosphate buffer at 20 mg/mL and obtains dark red-brown solutions. No
• solution stability data are currently available.
• STRUCTURE:
• Hemoglobin is a tetramer composed of 2 pairs of polypeptide chains called globins, and 4 heme groups.
• Each polypeptide chain is bound to one heme. Iron is coordinated to 4 pyrrole nitrogens of protoporphyrin IX
• and to an imidazole nitrogen of a histidine residue from the globin side of the porphyrin. The sixth
• coordination position is available for binding with other small molecules such as O 2 , CO or CO 2 ; the
• hemoglobin distorts in the process. Adult human hemoglobin consists of 96.5-98.5% HbA 1 (a 2 &sig; 2 dimer) and
• 1.5-3.5% HbA 2 (a 2 d 2 dimer), where a, &sig; and d refer to subunits with different amino acid sequences. 1,2,3
• NOMENCLATURE OF HEMOGLOBIN FORMS:
• 1.  Ferrihemoglobin, also called methemoglobin, refers to hemoglobin which contains iron in the +3
• oxidation state (Fe 3+ ).
• 2.  Ferrohemoglobin, also called reduced hemoglobin, refers to hemoglobin which contains iron in the +2
• (or reduced) oxidation state (Fe 2+ ). Hemoglobin must be in the reduced form to bind oxygen or other
• small molecules:
• a. Oxyhemoglobin (HbO 2 ) contains bound oxygen;
• b. Deoxyhemoglobin (Hb) does not contain bound oxygen;
• c. Carboxyhemoglobin (HbCO) contains carbon monoxide, which has displaced oxygen. The affinity
• of Hb for CO, a poisonous gas, is 325 times greater that its affinity for O 2 . 
•  
•  
• METHOD OF PREPARATION:
• Hemoglobin is usually prepared by separating red blood corpuscles from the lighter plasma components by
• centrifugation. The plasma is siphoned off and ether is added to the corpuscle paste, causing the cells to
• burst. Another centrifugation removes the ruptured cell envelopes, and leaves a clear red solution of
• hemoglobin. 1 References for methods of preparation of oxyhemoglobin (HbO 2 ) from horse, dog and human
• erythrocytes have been published. 1
• PRODUCT DESCRIPTION:
• Hemoglobin is the major component of red blood cells, and is responsible for their red color. Its normal
• concentration in erythrocytes is 34%. Hemoglobin is the most important respiratory protein of vertebrates
• by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport
• of carbon dioxide. The hemoglobin of all human races and chimpanzees are identical. Anomalous globins
• in which various amino acids have been substituted with others, or in which certain amino acids are missing
• entirely from the normal sequence, comprise 153 abnormal hemoglobin species. Some of these are
• responsible for diseases, the most common of which is sickle cell anemia - a condition which affects about
• 10% of Americans of African ancestry. In sickle cell hemoglobin (HbS), a valine residue has replaced the
• glutamic acid residue at position 6 in the &sig;-chain of normal Hb; the a-chain is normal. About 0.5% of all
• humans carry a mutant hemoglobin. 2,3
• PREPARATION OF REDUCED HEMOGLOBIN (HbO 2 ) FROM OXIDIZED HEMOGLOBIN: 5
• 1.  Equilibrate a 25 X 2.5 cm column of Sephadex G-25 with 20 mM phosphate buffer, pH 7.0, containing
• 10 -3 M EDTA.
• 2.  Apply to the column 2 mL of the same buffer to which 200 mg of sodium dithionite have been added,
• and help it drain into the gel by adding 1 mL of the phosphate buffer.
• 3.  Apply to the column about 10 mL of sample containing oxidized hemoglobin and elute with the
• phosphate buffer.
• 4.  Saturate the reduced hemoglobin eluent with oxygen gas.
• 5.  Dialyze the oxygenated eluent against oxygen-saturated phosphate buffer to eliminate excess
• dithionite and achieve complete conversion to oxyhemoglobin.
• REFERENCES:
• 1.   Index, 12th Ed., S. Budavari, Ed., p. 794, # 4682 (1996).
• 2.  T. Scott and M. Eagleson, Concise Encyclopedia: Biochemistry, 2nd Ed., pp. 255-259, Walter de
• Gruyter Press, New York (1988).
• 3.  A. L. Lehninger, Biochemistry, 2nd Ed., p. 111, Worth Publishers, Inc., New York (1975).
• 4.  A. Conway-Jacobs and L. M. Lewin, Anal. Biochem., 43, 394 (1971).
• 5.  H.B.F. Dixon and R. McIntosh, Nature, 213, 399 (Jan. 28, 1967).
• 6.  Benesh, R.E., R. Benesh and S. Yung, Anal. Biochem.

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