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  • 1
    Electronic Resource
    Electronic Resource
    Inter- and Intramolecular Interactions of α-Lactalbumin. II. Aggregation Reactions at Acid pH* (1964)
    s.l. : American Chemical Society
    Biochemistry 3 (1964), S. 1152-1160 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00896a025
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  • 2
    Electronic Resource
    Electronic Resource
    Zone electrophoresis of ''lichenase''
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 96 (1962), S. 187-188 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(62)90470-8
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  • 3
    Electronic Resource
    Electronic Resource
    PYROGLUTAMYL DIPEPTIDES IN MUSHROOM, AGARICUS CAMPESTRIS (1970)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY: A small fraction, containing evidence for the presence of pyroglutamyl dipeptides and an N-pyroglutamylhexosamine. was isolated from the edible, commercial mushroom. Agaricus campestris. Upon hydrolysis, this isolate liberated a copious amount of glutamic acid, together with smaller quantities of other amino acids and a hexosamine. Analyses of the unhydrolyzed and hydrolyzed portions of the fraction by an automatic amino acid analyzer revealed the identities and quantities of the compounds released. Additional chemical and physical methods of analysis gave supporting evidence for the presence in the mushroom in addition to proline and pyroglutamic acid of the pyroglutamyl dipeptides of threonine, aspartic acid, valine, leucine, citrulline, phenylalanine, glycine, alanine, glutamic acid and proline and also of the amino acid sugar, N-pyroglutamylglucosamine. Pyroglutamylcitrulline and N-pyroglutamylglucosamine were tentatively identified. The first 6 dipeptides are reported for the first time. A mechanism is proposed for the enzymic biosynthesis of the pyroglutamyl dipeptides in the mushroom. Results of the present work shed additional light on the complex nature of the higher basidiomycetes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1970.tb12122.x
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and Characterization of a Trypsin-Like Enzyme with Fibrinolytic Activity Present in the Abdomen of Horn Fly, Haematobia irritans irritans (Diptera: Muscidae) (2000)
    Springer
    The protein journal 19 (2000), S. 515-521 
    Details
    ISSN: 1573-4943
    Keywords: trypsin-like enzyme ; fibrinolytic activity ; protein purification ; hematophagous ; Haematobia irritans irritans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This work describes the purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of Haematobia irritans irritans (Diptera: Muscidae). The enzyme was purified using a one-step process, consisting of affinity chromatography on SBTI-Sepharose. The purified protease showed one major active proteinase band on reverse zymography with 0.15% gelatin, corresponding to a molecular mass of 25.5 kDa, with maximum activity at pH 9.0. The purified trypsin-like enzyme preferentially hydrolyzed synthetic substrates with arginine residue at the P1 position. The K m values determined for three different substrates were 1.88 × 10−4, 1.28 × 10−4, and 1.40 × 10−4 M for H-α-benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide (S2222), dl-Ile-Pro-Arg-p-nitroanilide (S2288), and DL-Phe-Pip-Arg-p-nitroanilide (S2238), respectively. The enzyme was strongly inhibited by typical serine proteinase inhibitors such as SBTI (soybean trypsin inhibitor, K i = 0.19 nM) and BuXI (Bauhinia ungulata factor Xa inhibitor, K i = 0.48 nM), and less inhibited by LDTI (leech-derived tryptase inhibitor, K i = 1.5 nM) and its variants LDTI 2T and 5T (0.8 and 1.5 nM, respectively). The most effective inhibitor for this protease was r-aprotinin (r-BPTI) with a K i value of 39 pM. Synthetic serine protease inhibitors presented only weak inhibition, e.g., benzamidine with K i = 3.0 × 10−4 M and phenylmethylsulfonyl fluoride (PMSF) showed traces of inhibition. The purified trypsin-like enzyme also digested natural substrates such as fibrinogen and fibrin net. The protease showed higher activity against fibrinogen and fibrin than did bovine trypsin. These data suggest that the proteolytic enzyme of H. irritans irritans is more specific to proteins from blood than are the vertebrate digestive enzymes. This enzyme's characteristics may be an adaptation resulting from the feeding behavior of this hematophagous insect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026557600429
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  • 5
    Electronic Resource
    Electronic Resource
    Continuous culture of Aspergillus phoenicis QM 329 for the production of cellobiase (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 2747-2751 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260241214
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