## Abstract **BACKGROUND:** Human erythropoietin (hEPO), a hydrophobic acidic glycoprotein responsible for the regulation of red blood cell production in mammals, is used for the treatment of anemia. In general, the purification of transgenic animalβderived therapeutic proteins is not easy due to t
Purification of human lysozyme from milk and pancreatic juice
β Scribed by Chi-Sun Wang; Hans-Ulrich Kloer
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 343 KB
- Volume
- 139
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Human milk lysozyme was purified by heparin-Sepharose affinity chromatography and Sepharose 4B gel-permeation chromatography. This procedure was also found applicable to the purification of human pancreatic juice lysozyme. Double-diffusion analyses indicated that human milk lysozyme was immunochemically identical to human saliva and human pancreatic juice lysozyme. Based on the identity of the N-terminal 10-amino-acid-residue sequence analyzed, it was suggested that human milk lysozyme and human pancreatic juice lysozyme are identical molecular entities.
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