Conformational studies of bacterial peptidoglycan: structure and stereochemistry of N-acetyl-β-d-glucosamine and N-acetyl-β-d-muramic acid
✍ Scribed by P.N.S. Yadav; D.K. Rai; J.S. Yadav
- Book ID
- 107803096
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 1020 KB
- Volume
- 194
- Category
- Article
- ISSN
- 0022-2860
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K,-cells from Drosophila melanogaster, grown under serum-free conditions, produce two p-hexosaminidases and secrete these enzymes into the medium. The two enzymes were separated by DEAE-exchange chromatography. According to their substrate specificities one enzyme is a f3-N-acetyl-D-glucosarninidase
O-(N-Acetyl-~-muramyl-L-alanyl-D\_isoglutamine)-(1~4)-~-acetyl-D-glucosamine (3, the re--peating disaccharide dipeptTde unit %tained by endo-&acetylglucos%minidase lysis of bacterial cell walls, has been synthesized in a twelve-step sequence from g-acetyl-g-glucosamine.
Kc-cells from Drosophila produce two different beta-D-hexosaminidases, a beta-N-acetyl-D-glucosaminidase (E.C.3.2.1.30) and a beta-N-acetyl-D-hexosaminidase (E.C.3.2.1.52), which are also secreted into the medium. The Mr of both enzymes is about 126,000 +/- 9,700; the S-values are 8.37 +/- 0.44. Bot