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Dechlorination and spectral changes associated with bacterial degradation of 2-(2-methyl-4-chlorophenoxy)propionic acid (1991)

Kelly, Martin P. ; Heniken, Michael R. ; Tuovinen, Olli H.

Springer

Journal of industrial microbiology and biotechnology 7 (1991), S. 137-145

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ISSN: 1476-5535

Keywords: Phenoxyherbicide ; Mecoprop degradation ; Biodegradation ; Mixed cultures

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Summary The bacterial degradation of mecoprop (2-(2-methyl-4-chlorophenoxy)propionic acid) was studied using a mixed culture under aerobic conditions. The release of chlorine from mecoprop indicated incomplete degradation (75%), which did not proceed to completion upon extended incubation. The UV absorbance initially increased and this was associated with spectral distortion of the shoulder and trough regions and a slight shift in the maximum wavelength of absorption. GC-MS analysis indicated that 4-chloro-2-methylphenol was an intermediate in the degradative pathway of mecoprop. The GC-MS data also suggested the formation of other phenolic compounds with repositioned chloro-and methylgroups.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01576076

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Heterotrimeric configuration is essential to the adhesive function of laminin (1992)

Lissitzky, J. C. ; Cantau, P. ; Martin, P. M.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 48 (1992), S. 141-149

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ISSN: 0730-2312

Keywords: laminin ; structure-function ; adhesion ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Mouse PFHR9 laminin, B1B2-heterodimers, and free B1-chains were separated from one another by gel filtration on superose 6. The cell attachment promoting activity of these species was measured after immunoprecipitation with monoclonal anti-laminin antibodies coupled to Sepharose 6MB beads. These antibodies, Which did not react with the laminin E8 fragment, were directed against epitopes in the NH2-terminus of the laminin B1-chain and in the central region of laminin. After incubation with purified EHS laminin, the immunosorbents revealed efficient adhesion substrates for a rat rhabdomyosarcoma cell line which attached preferentially to the laminin E8 fragment. Although both were immunoprecipitated efficiently, B1B2-heterodimers and B1-chains, unlike PFHR9 laminin, did not support the attachment of RMS cells. On a molar basis B1B2-heterodimers were 24 times less efficient than PFHR9 laminin or EHS laminin in supporting cell attachment. These data suggest that heterotrimeric configuration is essential to the adhesive function of the laminin E8 fragment.

Additional Material: 5 Ill.