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Biomedical subjects

E L BECKER

Publications and source records attributed to E L BECKER.

At least 19 recordsLinked to original sources
PubMed1964

A COMPARISON OF THE SPECIFICITY OF INHIBITION BY PHOSPHONATE ESTERS OF THE FIRST COMPONENT OF COMPLEMENT AND THE ANTIGEN-INDUCED RELEASE OF HISTAMINE FROM GUINEA PIG LUNG.

The ability of a number p-nitrophenylethyl alkyl, phenyl alkyl, chloroalkyl, and aminoalkyl phosphonates to inhibit the activated first component (C'1a) of guinea pig complement, and the antigen-induced release of histamine from sliced, perfused guinea pig lung has been compared. C'1a in its reactivity with these phosphonates is distinctly more similar to trypsin than to any of the other enzymes studied previously. It is suggested that both trypsin and C'1a possess an anionic group in the active center of the respective enzyme, but the distance between the anionic and esteratic site in C'1a might be less than in trypsin. The pattern of inhibition of histamine relase by the alkyl, phenyl alkyl, and chloroalkyl phosphonates is similar to the inhibition of C'1a by these compounds, although distinct differences are apparent. The aminoalkyl phosphonates are distinctly less active inhibitors of histamine release than the corresponding alkyl phosphonates, whereas the reverse is true of the inhibition of C'1a. On the basis of these differences, it is tentatively concluded that the organophosphorus-inhibitable enzymes in the guinea pig systems studied here are similar but not identical.

Animals↗
PubMed1964

FOREWORD.

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Bacteriology↗
PubMed1963

PEPSIN DIGESTION OF RABBIT AND SHEEP ANTIBODIES. THE EFFECT ON COMPLEMENT FIXATION.

7S sheep antibody is similar to 7S rabbit antibody, insofar as it too can be digested with pepsin to yield a 5S fragment still capable of precipitating homologous antigen. The 5S fragment from rabbit as well as sheep antibody is capable of fixing guinea pig complement. However, this fixation differs from the fixation by 7S antibody, since preformed antibody-antigen aggregates containing either sheep or rabbit 5S antibody fix only a maximum of 20 to 40 per cent of the total complement. The portion of complement which is fixable by the 5S preformed aggregates seems to be different from the remainder of the complement. Prior treatment of guinea pig serum with 5S washed preformed aggregates removes that portion of complement fixable by 5S antibody, and will leave the complement remaining unable to be fixed by further addition of 5S immune aggregates. Such absorbed complement, however, is as capable as is unabsorbed complement of being fixed by 7S antibody. The 5S sheep and rabbit antibody fixes the portion of complement which it is capable of fixing, as well as or better than the corresponding 7S antibody fixes the total complement. 5S preformed aggregates are broken down by treatment with cysteine, and their complement-fixing ability is lost.

Animals↗
PubMed1963

Complement-fixing properties of pepsin-treated rabbit and sheep antibodies.

Rabbit antibody with a sedimentation coefficient of 7S was digested with pepsin to yield the 5S fragment. Washed specific precipitates of 5S antibody and egg albumin, when added to guinea pig serum, fixed up to 40 percent of the total complement. This fixation could not be attributed to contamination with 7S antibody. Absorption of guinea pig serum with washed precipitates of 5S antibody and antigen removed that portion of complement which was fixed by fresh 5S antibody-antigen aggregates, but not that fixed by 7S antibody-antigen aggregates. The presence of 0.001M ethylenediaminetetraacetic acid prevented this absorption of complement by the 5S aggregates.

Animals↗