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          • 批發 牛血紅蛋白 現貨
          產品名稱:

          批發 牛血紅蛋白 現貨

          產品品牌: SOLARBIO/索萊寶 價格:
          廠商性質: 生產廠家 產品時間: 2025-04-23
          批發 牛血紅蛋白 現貨
          貨號:H8020
          規格:5g/瓶
          CAS:9008-02-0
          儲存條件:干燥保存
          外觀(性狀):深紅色結晶性粉末。
          單位:瓶

          產品概述

          品牌SOLARBIO/索萊寶

          批發 牛血紅蛋白 現貨
          貨號:H8020
          規格: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):深紅色結晶性粉末。
          • 單位:瓶

          ?

          • 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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