Searched for: author%3A%22Cohen%2C+J.A.%22
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1969
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1969
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1968
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Cohen, J.A. (author), Oosterbaan, R.A. (author), Berends, F. (author), Medisch Biologisch Laboratorium TNO (author)
bookPart 1967
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
bookPart 1967
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Daems, W.T. (author), Eigner, J. (author), van der Sluys, I. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1962
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Daems, W.T. (author), van de Pol, J.H. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1961
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van de Pol, J.H. (author), Veldhuisen, G. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1961
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Benoiton, L. (author), Rydon, H.N. (author), Oosterbaan, R.A. (author), van Adrichem, M.E. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
IN 1958, two of us1 obtained, by enzymic degradation of acetyl-chymotrypsin labelled with carbon-142, five peptides containing labelled acetyl-groups. Subsequent sequence studies3 have shown that the largest of these peptides has the amino-acid sequence, Gly.Asp.Ser.Gly.Gly.Pro.Leu, identical with that already found4, by degradation of the di...
article 1960
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van Arkel, G.A. (author), van de Pol, J.H. (author), Cohen, J.A. (author), Florkin, M. (author), Medisch Biologisch Laboratorium TNO (author)
article 1960
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Welling, W. (author), Cohen, J.A. (author), Berends, W. (author), Medisch Biologisch Laboratorium TNO (author)
The effect of a very toxic agent with antibiotic properties (bongkrekic acid), produced by Pseudomonas cocovenenans, on the oxidation of citric acid cycle intermediates catalyzed by heart muscle tissue has been investigated. It was found that the oxidation of pyruvate, α-ketoglutarate and malate was inhibited, whereas oxidation of succinate and...
article 1960
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Welling, W. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1960
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
conference paper 1960
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Jansz, H.S. (author), Posthumus, C.H. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
Horse-liver ali esterase reacts with DFP to form the enzymically inactive DP-enzyme. With isonitrosoacetone diisopropylphosphate is released from the inhibited enzyme; this is accompanied by a recovery of the enzymic activity. In order to investigate the chemical nature of the DFP-binding site of ali esterase the DP-enzyme was digested with...
article 1959
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Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
article 1959
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Cohen, J.A. (author), Oosterbaan, R.A. (author), Jansz, H.S. (author), Berends, F. (author), Medisch Biologisch Laboratorium TNO (author)
article 1959
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van Bekkum, D.W. (author), Vos, O. (author), Brocades Zaalberg, O. (author), Weyzen, W.W.H. (author), de Vries, M.J. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
conference paper 1959
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Jansz, H.S. (author), Posthumus, C.H. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
The structure of a diisopropylphosphoryl-containing peptide obtained by digestion of DFP-inhibited horse-liver ali esterase by pepsin was established as follows: gly-glu-DP·O·ser-ala-gly-gly-(glu, ser). © 1959.
article 1959
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Oosterbaan, R.A. (author), Kunst, P. (author), van Rotterdam, J. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
1. 1. After reaction with DF32p, α-chymotrypsin was subjected to a proteolytic digestion. From the digest two related peptides containing the radioactive diisopropylphosphoryl-group were isolated. 2. 2. The amino acid composition of one peptide was established as aspartic acid or asparagine (1), serine (1), glycine (3), and proline (1). In...
article 1958
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Oosterbaan, R.A. (author), Kunst, P. (author), van Rotterdam, J. (author), Cohen, J.A. (author), Medisch Biologisch Laboratorium TNO (author)
1. 1. The amino acid sequence of two diisopropylphosphoryl-substituted peptides obtained from α-chymotrypsin-DP by enzyme hydrolysis was established as: glycyl-aspartyl-seryl-glycyl-glycyl-prolyl-leucine and glycyl-aspartyl-seryl-glycyl-glycyl-proline, respectively. 2. 2. The experimental results strongly suggest that the diisopropylphosphoryl...
article 1958
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