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  • 1
    Electronic Resource
    Electronic Resource
    Clitidine, a new toxic pyridine nucleoside from clitocybe acromelalga
    Amsterdam : Elsevier
    Tetrahedron 38 (1982), S. 3281-3284 
    Details
    ISSN: 0040-4020
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0040-4020(82)80107-5
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  • 2
    Electronic Resource
    Electronic Resource
    Estimate of the source of soil protease in upland fields (1994)
    Springer
    Biology and fertility of soils 18 (1994), S. 341-346 
    Details
    ISSN: 1432-0789
    Keywords: Soil protease ; Andosol ; Gray Lowland soil ; Bacillus spp ; Proteolytic bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Selective inhibition of bacterial or fungal growth in remoistened, oven-dried, inoculated Andosols indicated that bacteria were a more important source of benzyloxycarbonyl-l-phenylalanyl-l-leucine hydrolyzing activity (z-FLase) and casein-hydrolyzing activity (caseinase) than fungi. The same test indicated that bacteria were also a more important source of soil caseinase under upland conditions in a Gray Lowland soil. Most of the proteolytic bacteria isolated from the three upland fields by azocoll agar plates (Andosol upland field, 100%; Andosol uncultivated field, 96.4%; Gray Lowland upland field, 70.0%) wereBacillus spp. Most (100%, 97.1%, and 84.0%, respectively) of the gelatin liquefiers selected from the azocoll degraders, as those with high extracellular z-FLase and caseinase, were alsoBacillus spp. We conclude thatBacillus spp. are the major source of soil protease in the three upland fields studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570638
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a metalloproteinase component extracted from soil (1987)
    Springer
    Biology and fertility of soils 4 (1987), S. 179-183 
    Details
    ISSN: 1432-0789
    Keywords: Proteinases ; Metalloproteinase ; Soil enzyme ; Soil extract ; Nitrogen transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary A metalloproteinase was found to be the main component of a protease in the extract from an Andosol collected from a tomato field. The protease has a pH optimum of 7 for benzyloxycarbonyl-L-phenylalanyl-L-tyrosyl-L-leucine with tyrosylleucine as the main reaction product. The Km value for the substrate was 0.4 mM. Activity was inhibited by EDTA but not by pepstatin, p-chloromercuribenzoate and phenylmethanesulfonyl fluoride. After the removal of EDTA from the inactivated enzyme by dialysis and the addition of metal ions (Zn2+, Mn2+ and Fe3+), the enzyme activity could be recovered. The apparent isoelectric points of the metalloproteinase components were estimated to be 4.9, 4.5 and 4.1 by isoelectric focusing. A fraction with an apparent isoelectric point of 4.9 was the main component. The apparent molecular weight of the main protease component was estimated to be 4.7 × 104 by gel filtration of Sephadex G-100. The enzyme hydrolyzed a natural polypeptide, angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu). Main split sites in the peptide were -Tyr7-Ile5- and -Pro7-Phe8-. The former was the most sensitive site to the soil metalloproteinase concerned.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270938
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  • 4
    Electronic Resource
    Electronic Resource
    Populations of methanogenic bacteria in paddy field soil under double cropping conditions (rice-wheat) (1995)
    Springer
    Biology and fertility of soils 20 (1995), S. 113-117 
    Details
    ISSN: 1432-0789
    Keywords: Methanogenic bacterial population ; Paddy field soil ; Double cropping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The methanogenic populations able to use H2−CO2, methanol, and acetate were investigated in paddy field soil in situ under double cropping conditions [rice (Oryza sativa L.) as a summer crop under flooded conditions and wheat (Triticum aestivum L.) as an upland winter crop] over 2 years approximately bimonthly by the most probable number method. Three fields, one without fertilizer, one treated with inorganic fertilizer (mixed fertilizer including urea, ammonium phosphate, and potassium sulfate), and one treated with wheat straw plus inorganic fertilizer, were examined. The population of H2−CO2, methanol, and acetate utilizers in the paddy field soil at a depth of 1–6 cm was 103–104, 104–105, and 104–105 g-1 dry soil, respectively. These values were almost constant during the 2 years irrespective of moisture regime (flooded or nonflooded), crop (rice or wheat), fertilizer treatment, and soil depth (0–1, 1–10, and 10–20 cm).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00336589
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of a phosphodiesterase component in a forest soil extract (1987)
    Springer
    Biology and fertility of soils 3 (1987), S. 159-164 
    Details
    ISSN: 1432-0789
    Keywords: A bis-(p-nitrophenyl) phosphatase (BPNPase) ; Forest soil extract ; Fractionation on DEAE-cellulose column chromatography ; Oligonucleotides ; Cyclic nucleotides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary A bis-(p-nitrophenyl) phosphatase (BPN-Pase) was extracted from a forest soil and fractionated by DEAE-cellulose column chromatography into seven fractions (1, 2, 3, 4, 5, 6 and 7). The main fraction (fraction 5) was further fractionated into 3 subfraction (fractions 1, 2 and 3) by affinity chromatography for nuclease. The properties of the BPNPase in subfraction 3 were characterized and the results are reported in this article. Subfraction 3, which had a peak at about 278 run in the UV absorption spectrum, hydrolyzed 2′,3′-cyclic-nucleotides more readily than 3′,5′-cyclicnucleotides, adenylyl-(3′ → 5′)uridine, uridylyl-(3′ → 5′)adenosine, thymidine 3′-p-nitrophenyl phosphate, thymidine 5′-p-nitrophenyl phosphate, p-nitrophenyl phosphate and BPNP. Subfraction 3 hydrolyzed BPNP into 2 mol p-nitrophenyl and 1 mol inorganic phosphate during incubation. Apparent molecular weight of the BPNPase was estimated to be about 58 000 by gel filtration. The BPNPase activity had a pH optimum at 5.0 and was inhibited by Hg2+ and slightly inhibited by F− and PO 4 3− . These observations suggest that the BPNPase is subfraction 3 has been constituted mainly with 2′,3′cyclic-nucleotide 2′-phosphodiesterase [EC 3.1.4.16] or 2′,3′-cyclic-nucleotide 3′-phosphodiesterase [EC 3.1.4.37].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00255777
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  • 6
    Electronic Resource
    Electronic Resource
    Properties of protease extracted from tea-field soil (2000)
    Springer
    Biology and fertility of soils 30 (2000), S. 351-355 
    Details
    ISSN: 1432-0789
    Keywords: Key words Tea-field soil ; Soil protease ; Serine-carboxypeptidase ; Metallocarboxypeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract  Crude enzyme extract was obtained from a low-pH soil from a tea field by shaking with 0.1 M PO4 3– buffer (pH 7.0). Hydrolytic activity toward benzyloxycarbonyl-L-Phe-L-Leu (Z-L-Phe-L-Leu) and Z-L-Phe-L-Tyr-L-Leu showed two pH optima, at about pH 5 and 9, suggesting that the soil contained at least two protease components. The acid-type protease in the extract was assumed to be Ser-carboxypeptidase because phenylmethanesulphonyl fluoride and diisopropylphosphoro fluoridate inhibited its activity. Peptide bonds in the C-terminal residues of Leu-enkephalin and angiotensin I were split more by protease than those in the N-terminal residue. The apparent molecular weight of the acid-type protease was estimated to be 75 kDa by Sephadex G-100 gel filtration and the isoelectric point 4.4 by isoelectric focusing. A neutral-type protease in the extract was assumed to be a metallocarboxypeptidase because only o-phenanthrorine inhibited its activity. Peptide bonds in the C-terminal residues of Leu-enkephalin and angiotensin I were hydrolyzed to a greater extent than those in the N-terminal residues. The apparent molecular weight of the neutral-type protease was estimated to be 37 kDa and the isoelectric point 5.8, 8.0 and 9.4. The isoelectric point 9.4 fraction showed the highest relative activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003740050015
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  • 7
    Electronic Resource
    Electronic Resource
    Conformationally selective transannular cyclizations of humulene 9,10-epoxide. Synthesis of the two skeletally different cyclohumulanoids: dl-bicyclohumulenone and dl-africanol
    Amsterdam : Elsevier
    Tetrahedron Letters 21 (1980), S. 4835-4838 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0040-4039(80)80152-3
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  • 8
    Electronic Resource
    Electronic Resource
    Structure and synthesis of clitidine, a new pyridine nucleoside from clitocybe acromelalga
    Amsterdam : Elsevier
    Tetrahedron Letters 18 (1977), S. 481-482 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(01)92671-1
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  • 9
    Electronic Resource
    Electronic Resource
    Biogenetic-like conversion of Δ^7^(^8^)-protoilludene to hirsutene
    Amsterdam : Elsevier
    Tetrahedron Letters 19 (1978), S. 1991-1994 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(01)94729-X
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  • 10
    Electronic Resource
    Electronic Resource
    Seasonal variation in extracted proteases and relationship to overall soil protease and exchangeable ammonia in paddy soils (1996)
    Springer
    Biology and fertility of soils 21 (1996), S. 89-94 
    Details
    ISSN: 1432-0789
    Keywords: Extracted soil z-FLase ; Extracted soil caseinase ; Exchangeable NH 4 + ; Ninhydrin-reactive nitrogen ; Soil protease ; Wetland rice ; Crop rotation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract In paddy fields treated with organic manure or chemical fertilizer or not treated, seasonal changes in soil protease [hydrolysis to benzyloxycarbonyl-l−phenyl-alanyl-l−leucine (z-FLase) or casein (caseinase)] extracted with phosphate buffer were investigated during the cultivation of rice. Both activities reached a maximum on July 21 (after irrigation), and gradually decreased, which was correlated with the soil water content. Increases in z-FLase and caseinase activity extracted coincided with increases in exchangeable NH 4 + and the ninhydrin-reactive N content. The overall soil caseinase activity on August 16 (after midsummer drainage) was inhibited by metal chelators and p−chloromercuribenzoic acid and was similar to that extracted with 1.0 mol l−1 phosphate buffer on June 9 (before irrigation), but different from that extracted by 0.1 mol l−1 phosphate buffer on July 22. The overall soil z-FLase activity on August 16 was inhibited by p−chloromercuribenzoic acid and 1,10-phenanthroline, and was similar to that extracted with 0.1 mol l−1 phosphate buffer on June 9, but differed from that extracted on July 22. The results indicate that the soil proteases extracted on July 22 had a high potential for ammonification and were short lived.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00335998
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