Enzymatic hydrolysis of γ-glutamyl polypeptide and its derivatives

Kream, Jacob; Borek, Blanche Ann; DiGrado, C.Joseph; Bovarnick, Max

doi:10.1016/0003-9861(54)90414-2

Cited by 8 publications

(3 citation statements)

References 10 publications

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“…Like the enzvme system found in human red blood cells and tissues (Kream et al, 1954), the bacterial enzyme attacks the L-configuration only; in this respect, both differ from the enzyme produced by B. subtilis (Thorne et al, 1954) which preferentially hydrolyzes the poly-Dglutamic acid. On the other hand, the enzymes described by Kream et al., and by Thorne et al, form small quantities of short peptides, while the F. polyglutamicum enzyme does not.…”

Section: Discussionmentioning

confidence: 92%

“…Part of a thesis submitted by P. Margalith to the Hebrew University, Jerusalem, in partial fulfilment of the requirements for the degree of Doctor of Philosophy.2 Not long after this work was began, Thorne et at. (1954) found, in culture-filtrates of Bacillus subtilis, an enzyme that hydrolyzes the native glutamyl polypeptides;Kream et al (1954) found a similar enzyme in human red blood cells and in various tissues. However, the specificity of these enzymes to substrates other than polyglutamic acid was not reported.…”

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confidence: 97%

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A NEW SPECIES ( FLAVOBACTERIUM POLYGLUTAMICUM ) WHICH HYDROLYZES THE γ- l -GLUTAMYL BOND IN POLYPEPTIDES

Volcani

Margalith

1957

J Bacteriol

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It has been shown (Kovacs and Bruckner, 1952; Bruckner et al., 1953a, 1953b, 1953c) that certain bacteria produce glutamyl polypeptides in which the y-glutamyl bond predominates; that produced by Bacillus anthracis (Ivainovics and Erd6s, 1937; Ivanovics and Bruckner, 1937; Hanby and Rydon, 1946) and by Bacillus mesentericus (Bruckner and Ivdnovics, 1937) contains the D-isomer alone, whereas that formed by Bacillus subtilis (Bovarnick, 1942) contains both D-and L-isomers in varying quantities (Thorne et al., 1954). Confirmatory evidence for the presence of the 'y-glutamyl bond has been provided recently by work with synthetic 'y-poly-L-(Waley, 1955; Bruckner et al., 1955a) and-y-poly-D-glutamic acid (Bruckner et al., 1955b). Other natural products in which y-glutamyl residues occur include pteroylglutamic acid conjugates and p-aminobenzoylpolyglutamic acid. These substances are important growth factors and are split by conjugases (Stokstad, 1954). It was thought that an organism that can grow on the bacterial polypeptide and can specifically split the 'y-glutamyl linkages might serve as the source of an enzyme to demonstrate the existence of 'y-glutamyl bonds in proteins.2 Indeed, it has been reported (Haurowitz and Bursa, 1949) that 'y-linked glutamic acid occurs in proteins, but this has not been conclusively demonstrated since there is as yet no reliable method for distinguishing between a-and-y-bonds in protein; an improved chemical method was recently described by Haurowitz and Horowitz (1956).

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Section: Discussionmentioning

confidence: 92%

mentioning

confidence: 97%

A NEW SPECIES ( FLAVOBACTERIUM POLYGLUTAMICUM ) WHICH HYDROLYZES THE γ- l -GLUTAMYL BOND IN POLYPEPTIDES

Volcani

Margalith

1957

J Bacteriol

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“…Plasma proteins were determined by Kjeldahl nitrogen analyses of the dissolved (in 2 N NaOH) washed, trichloracetic acid precipitate of heparinized plasma samples. Concentration of the polymer in plasma was determined by the method previously described (8).…”

Section: Methodsmentioning

confidence: 99%

Efficiency of Glutamyl Peptide Polymers as Plasma Volume Extenders

Rosenthal

O’Connell

Axelrod

et al. 1956

The Journal of Experimental Medicine

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A series of polymers of polyglutamic acid have been tested as plasma volume expanders. The results indicate that those polymers prepared from backbones of 40,000 molecular weight or over and side chains of 3,000 molecular weight or over, will have plasma volume retention half-life of 15 hours or longer. Measurements of the oncotic efficiency of these polymers in vivo indicated a blood stream fluid retention of approximately 51 ml./gm. of polymer. Similar measurements of polymer-serum albumin solutions in vitro showed a retention of 52 ml./gm. of polymer. The clinical response to infusion of solutions of these polymers indicated no untoward pharmacological properties. Although the number of trials presented is too small for ultimate conclusion regarding either the physiological or clinical effects of these polymers, they do provide a strong indication of the desirability of further clinical testing of this polymer and a sound basis on which to plan the larger scale preparation of polymer. Both measures are currently under way.

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