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骆驼肌红蛋白

Camel myoglobin.

作者信息

Awad E S, Kotite L

出版信息

Biochem J. 1966 Mar;98(3):909-14. doi: 10.1042/bj0980909.

Abstract
  1. Crystalline myoglobin was prepared from camel heart muscle. 2. A method was developed for the isolation of myoglobin that employs molecular-sieve chromatography. 3. Analytical chromatography of the camel myoglobin on a molecular-sieve column and on two types of ion-exchange columns gave in each case a single elution band, which accounted for better than 98% recovery and showed that the product was free from haemoglobin. 4. The iron content on a dry weight basis was 0.308%. This value corresponds to a molecular weight of 18100. 5. The spectra of acidic ferrimyoglobin, basic ferrimyoglobin and ferrimyoglobin cyanide were measured. 6. The pK(a) of the dissociation of the haem-bound water molecule in acidic ferrimyoglobin was 8.53 at 25 degrees . 7. Conclusions are drawn about the charge on the surface of the camel ferrimyoglobin molecule as compared with horse and sperm-whale ferrimyoglobins.
摘要
  1. 结晶肌红蛋白是从骆驼心肌中制备的。2. 开发了一种采用分子筛色谱法分离肌红蛋白的方法。3. 在分子筛柱和两种离子交换柱上对骆驼肌红蛋白进行分析色谱分析,每种情况下均得到单一洗脱峰,回收率高于98%,表明产物不含血红蛋白。4. 以干重计铁含量为0.308%。该值对应分子量为18100。5. 测量了酸性高铁肌红蛋白、碱性高铁肌红蛋白和高铁肌红蛋白氰化物的光谱。6. 酸性高铁肌红蛋白中血红素结合水分子解离的pK(a)在25℃时为8.53。7. 得出了骆驼高铁肌红蛋白分子表面电荷与马和抹香鲸高铁肌红蛋白相比的结论。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/80ce/1264936/96f1ea18c390/biochemj00757-0279-a.jpg

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