Changes in membrane protein during the development of macrocysts in Physarum polycephalum.

Fujishita, Shigeto; Morita, Masashi; Okamura, Shöji; Nishi, Arasuke

doi:10.2323/jgam.30.97

Cited by 3 publications

(1 citation statement)

References 8 publications

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“…In addition, aminopeptidases in vegetative plasmodia were suggested to be involved in the differential protein turnover during differentiation (13,31). Our previous work showed that the membrane-bound glycoproteins of this mould in the vegetative growing phase mostly disappears with induction of spherulation (12,17). The importance of some proteinases for the progress of sporulation has also been reported in other microorganisms (6,34).…”

Section: Discussionmentioning

confidence: 99%

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

Morita

Kan

Sugano

et al. 1996

J. Gen. Appl. Microbiol.

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A trypsin-like serine proteinase was found in a plasma membrane fraction from the plasmodia of Physarum polycephalum. It was solubilized from the plasma membrane fraction with 1% (w/v) Triton X-100 and purified by a series of column chromatographic steps followed by polyacrylamide gel electrophoresis (PAGE). The molecular mass of the enzyme was estimated to be 130 kDa by SDS-PAGE under non-reducing conditions. This enzyme exhibited maximal activity at pH 9 and at 35°C with the substrate Boc-Phe-Ser-Arg-MCA, and was sensitive to various serine proteinase inhibitors and trypsin inhibitors. The enzyme was significantly labeled with [3H]diisopropylfluorophosphate (DFP); however, a clear decrease in the amount of the enzyme bound-[3H]DFP was observed in the presence of p-nitrophenyl p'-guanidinobenzoate (NPGB), an active site titrant for trypsin. The activity was completely inhibited in the presence of EDTA or EGTA, but the metal-depleted enzyme was reactivated by the addition of Cart Moreover, this enzyme was capable of cleaving several synthetic peptides at the carboxyl side of arginine, but did not work on synthetic substrates for chymotrypsin, elastase and aminopeptidase. The enzyme showed an affinity to Con A, indicating that it contains a carbohydrate moiety. Inhibition of the activity by a serine proteinase inhibitor resulted in cessation of the DNA synthesis in growing plasmodia without loss of the protein synthesis. Thus, this trypsin-like serine proteinase may have a regulatory role in the growth and development of the slime mould.

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Section: Discussionmentioning

confidence: 99%

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

Morita

Kan

Sugano

et al. 1996

J. Gen. Appl. Microbiol.

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Isozyme polymorphism of cellulases in Aspergillus terreus

Singh¹,

Brar²,

Sandhu³

et al. 1996

J. Basic Microbiol.

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Maximum cellulase production in Aspergillus terreus was obtained at a temperature of 28 degrees C, pH 4.0 and a substrate concentration of 1% CMC. Variability in cellulase enzyme production and isozyme polymorphism of endo-beta-1,4-glucanase and beta-1,4-glucosidase was studied in 45 natural isolates of A. terreus. Different electrophoretic patterns were evident for endoglucanase. Three zones of activity viz EG 1, EG 11 and EG 111 were observed showing different electrophoretic mobilities. Some of the isolates exhibited the presence of null alleles for EG 1. During development EG 1 and EG 11 were observed throughout while EG 111 appeared on the eighth day. For beta-1,4-glucosidase two zones of activity viz beta-glu 1 and beta-glu 11 were observed. beta-glu 1 showed variable electrophoretic mobilities. beta-glu 1 appeared throughout during development while beta-glu 11 appeared on the twelfth day.

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Lipid-oligosaccharide intermediate of glycoprotein synthesis in Physarum polycephalum

Morita

Kurosaki

Nishi

1986

Biochimica et Biophysica Acta (BBA) - General Subjects

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Changes in membrane protein during the development of macrocysts in Physarum polycephalum.

Cited by 3 publications

References 8 publications

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

Isozyme polymorphism of cellulases in Aspergillus terreus

Lipid-oligosaccharide intermediate of glycoprotein synthesis in Physarum polycephalum

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