Multiple polypeptides immunologically related to ß-poly(L-malate)hydrolase (polymalatase)in the plasmodium of the slime mold Physarum polycephalum (Record no. 50088)

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control field 20250625160141.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-15912
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Title Multiple polypeptides immunologically related to ß-poly(L-malate)hydrolase (polymalatase)in the plasmodium of the slime mold Physarum polycephalum
490 0# - SERIES STATEMENT
Volume/sequential designation European Journal of BioChemistry, 251(1-2), p.405-412, 1998
520 3# - SUMMARY, ETC.
Summary, etc. Plasmodia of Physarum polycephalum contain large amounts of the cell-type-specific polyanion ß-poly(L-malate)and of a corresponding specific hydrolase (polymalatase), both expressed in the plasmodial form of the organism. We have partially purified polymalatase, the preparation consisting of several polypeptides, which could not be separated without destroying the hydrolase activity. Polypeptides of 68 kDa and 97 kDa were identified as polymalatases. Both were glycosylated, the 68-kDa form giving rise to a 54-kDa form when deglycosylated, and the 97-kDa form giving rise to an 88-kDa polypeptide that was indistinguishable from an 88-kDa inactive species also contained in the enzyme preparation. Antisera against each of these proteins were used to detect the intracellular distribution of the proteins. We found that the antisera crossreacted with the three proteins and, furthermore, with a multiplicity of polypeptides ubiquitously distributed over the plasmodium. Results of a two-dimensional non-denaturing in the first dimension and SDS-denaturing polyacrylamide gel electrophoresis in the second dimension suggested that the proteins were derived from a 200-kDa 'precursor' protein by proteolytic fragmentation. Polymalatase activity could be generated from a high molecular-mass precursor. According to several pieces of evidence, the proteolytic nicking occurred within plasmodia. The fragments were sticky and gave rise to preferred sizes of nicked macromolecules. The observed multiplicity varied as a function of the age of the cultures. The cellular distribution and the intracellular pH value were not compatible with an in situ polymalatase activity and suggested other, presently unknown, function(s)such as in the transportation of ß-poly(L-malate)from the nucleus to the culture medium.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element B-POLY(L-MALATE)
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element FRAGMENTATION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element IMMUNE CROSS-REACTIVITY
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHYSARUM POLYCEPHALAM
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element POLYMALATASE
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Karl, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Holler, E.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1RlKVDMkgiIqLnb0gBLWxWSFvC7LN_w5z/view?usp=drivesdk">https://drive.google.com/file/d/1RlKVDMkgiIqLnb0gBLWxWSFvC7LN_w5z/view?usp=drivesdk</a>
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-15912 25.06.2025 25.06.2025 Documentos solicitados