可破细胞壁 牛血红蛋白
货号:H8020
规格:5g/瓶
- 别名:Hb 牛血红蛋白 高铁血红蛋白 Hemoglobin
- 英文名称:Hemoglobin from bovine blood Hemoglobin
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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 .
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- 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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