Japanese journal of leprosy
Online ISSN : 2185-1360
Print ISSN : 0386-3980
ISSN-L : 0386-3980
On The Beta-Glucuronidase Binding Protein (BGBP) Of Microorganisms
Its Purification, The Antiserum Preparation Against That And Its Localization In Leproma And The Other Infectious Lesions Shown By Immunohistologic Method
Eiichi MatsuoAkio KomatsuSuguru MaekawaYukihiro FurunoAkiko MatsushitaAyumi SumiishiNorisuke SasakiOlaf K. Skinsnes
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1994 Volume 63 Issue 2 Pages 35-46

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Abstract
Our previous studies suggested that M. leprae (ML) grow in peripheral nerves and lepra cells because ML metabolize hyaluronic acid (HA), and use its component for their growth by the aid of host enzyme combined to the bacilli derived β-glucuronidase binding protein (BGBP). In this study, therefore, we examined the method to purify BGBP from a mycobacterium HI-75 originally separated from a leproma and cultured by modified Ogawa's medium containing split products of HA (glucuronic acid and N-acetylglucosamine). The distribution of BGBP in leproma and the other lesions consisting of hepatitis B virus infected liver and M. avium-intracellulare infected lung tissue were also immunohistologically examined.
As the result, the best method to get BGBP was preparatory electrophoresis in the final step of the purification and not the molecular sieving.
The BGBP was actually proven in leproma and the other infected tissues as described, indicating the abilities of these microorganisms to utilize the metabolic machinery of the host with the similar ways to that of ML.
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