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Clinically active bovine growth hormone fraction

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专利汇可以提供Clinically active bovine growth hormone fraction专利检索,专利查询,专利分析的服务。并且A clinically active component (TBGH-d) of a tryptic digest of bovine growth hormone (BGH) found to be homogeneous by disc electrophoresis and sedimentation equilibrium and having substantially the same molecular weight and amino acid composition as BGH was separated into two fractions, A-I and AII, by dextran gel filtration in 50 percent acetic acid. The amino acid analysis of the A-I and A-II fractions accounted for all the amino acids in the TBGH-d. The biological activity of the A-II fraction was found to be about 10-30 percent of TBGH-d. This fraction, having a molecular weight of about 5,000 and an amino acid content or chain length of 38 amino acids, appears to exhibit human growth hormone-like activity. This fraction also appears to have wider applicability than simply being useful for the acceleration of somatic growth in humans. For example, this fraction would appear to have utility in promoting increased function and growth in an impaired liver and in effecting tissue regeneration, such as the promotion of healing of stress ulcers. It would also appear that this fraction has utility in the stimulation of protein synthesis to increase immunological competence and in wound and fracture healing. Also, it would appear that this fraction has utility in non-human applications, e.g., for increasing milk production, for increasing wool production and for accelerating animal growth.,下面是Clinically active bovine growth hormone fraction专利的具体信息内容。

  • 2. A process in accordance with claim 1 wherein said dextran gel filtration is carried out in the presence of 50 percent acetic acid.
  • 3. A clinically active fraction produced in accordance with the process of claim 1, the amino acid content of said fraction being made up of lysin, arginine, aspartic acid and asparagine, threonine, serine, glutamic acid and/or glutamine, proline, glycine, alanine, valine, methionine, isoleucine, leucine, tyrosine and phenylalanine.
  • 4. A process in accordance with claim 1 wherein the trypsin digestion was stopped by the addition of soybean trypsin inhibitor.
  • 5. A process in accordance with claim 1 wherein said clinically active component is recovered from said tryptic digest upon diethylaminoethyl-cellulose chromatography by stepwise elution with aqueous ammonium bicarbonate having concentrations in the range of 0.03M through 0.15M.
  • 6. A process in accordance with claim 5 wherein said clinically active component is recovered upon elution with aqueous ammonium bicarbonate at a concentration of about 0.05M.
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