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  • 深红色结晶性粉末 牛血红蛋白
产品名称:

深红色结晶性粉末 牛血红蛋白

产品品牌: 索莱宝 价格:
厂商性质: 生产厂家 产品时间: 2024-01-17
深红色结晶性粉末 牛血红蛋白
货号:H8020
规格:5g/瓶
CAS:9008-02-0
储存条件:干燥保存
外观(性状):深红色结晶性粉末。
单位:瓶

产品概述

品牌SOLARBIO/索莱宝

深红色结晶性粉末 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
  • CAS:9008-02-0
  • 储存条件:干燥保存
  • 外观(性状):深红色结晶性粉末。
  • 单位: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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