PROTEINASE BIOSYNTHESIS BY STREPTOCOCCUS LIQUEFACIENS: I. THE EFFECT OF CARBON AND NITROGEN SOURCES, pH, AND INHIBITORS

Rabin, Robert; Zimmerman, Leonard N.

doi:10.1139/m56-088

Cited by 29 publications

(23 citation statements)

References 5 publications

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“…Such enzymes are usually inactivated by iodoacetate which carboxymethylates thiol groups, including those acting as zinc binding-sites. Native group D proteinase is not affected by iodoacetate (Rabin and Zimmerman, 1956), but EDTA-inactivated proteinase that is treated with the thiol poison cannot be reactivated. It appears, therefore, that chelation of the enzyme involves the exposure of such a susceptible site.…”

Section: Discussionmentioning

confidence: 99%

“…It was cultured always at 37 C. Media. A-C broth (Rabin and Zimmerman, 1956) was used to bring up the inoculum for the induction medium. The latter, N-Z Case synthetic medium, was constituted as follows: Sheffield N-Z Case, 0.2 g; L-arginine HCl, 0.193 g; lactose, 0.2 g; KH2PO4 1.0 g; NaCl, 0.2 g; MgSO4-7H20, 8 mg; FeSO4-7H20, 0.4 mg;…”

Section: Methodsmentioning

confidence: 99%

“…Group D streptococci also produce an extracellular proteinase. The enzyme was partially purified by Grutter and Zimmerman (1955), the metabolic optima for enzyme biosynthesis were determined (Rabin and Zimmerman, 1956;Hartman, Zimmerman, and Rabin, 1957), and biosynthetic control mechanisms were studied (Hartman and Zimmerman, 1960). The present communication details initial chemical studies of the enzyme, and presents data that indicate basic dissimilarities with the group A proteinase.…”

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confidence: 95%

“…Effect of iodoacetate on Zn++ reactivation. The thiol poison, iodoacetate, does not significantly affect native group D proteinase (Rabin and Zimmerman, 1956). The effect of the poison on Zn reactivation of EDTA-inactivated enzyme was studied in the following manner.…”

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confidence: 99%

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PROPERTIES OF PROTEINASE FROMSTREPTOCOCCUS FAECALISVAR.LIQUEFACIENS

Bleiweis

Zimmerman

1964

J Bacteriol

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BLEIWEIS, ARNOLD S. (The Pennsylvania State University, University Park), AND LEONARD N. ZIMMERMAN. Properties of proteinase from Streptococcus faecalis var. liquefaciens. J. Bacteriol. 88: 653-659. 1964.-The extracellular group D streptococcal proteinase is inactivated by chelating agents [ethylenediamine-tetraacetate (EDTA), ophenanthroline, and 8-quinolinol] and mercaptans (cysteine, mercaptoethanol, and thioglycolate).The optimal inhibitory concentrations of EDTA (4 X 1O4 M) and cysteine (2.5 X 1O2 M) promote rapid loss of activity with 50% inactivation after 4 to 5 min. Enzyme inactivated by either EDTA or

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 95%

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confidence: 99%

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PROPERTIES OF PROTEINASE FROMSTREPTOCOCCUS FAECALISVAR.LIQUEFACIENS

Bleiweis

Zimmerman

1964

J Bacteriol

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“…T h e method used to prepare the cell inoculum has been described in detail (18). A 10yo v/v cell inoculum was used.…”

Section: Introductionmentioning

confidence: 99%

The Effects of Oxygen and Carbon Dioxide on Proteinase Biosynthesis by Streptococcus Faecalis Var. Liquefaciens

Swiencicki¹,

Hartman²

1967

Can. J. Microbiol.

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The effect of 0 2 and COs on proteiriase biosynthesis by nonproliferating cells of Streptococc~is faecalis var. liquefacisrts in chenlically defined media were studied. I n the absence of COs,.Or (1% in N?) s t i~n~~l a t e d proteinase formatioil by promoting earlier synthesis and by increasing the rate of enzyme biosynthesis. Carbon dioxide ~~n d e r anaerobic conditions only enhariced the rate of protciilase synthesis. The sti~u~ilatory effect of the two gases was not additive. Glucose SLIPported a greater yield of proteinase than galactose under all conclitions of 0 2 and COL availability. Galactose \vns stinl~~latory in the presence of glucose only ~inder aerobic conditions (1% 0 2 in N?) when atinosphcric CO? \vas removed. Oxygen a t the 20% level inhibitetl proteinase formation by increasing the rate of arginine disappearance from the medi~im. IntroductionNutritional aspects of proteinase biosynthesis by nonproliferatiilg cells of Streptococciis faecalis var. liq~iefaciens in static culture under a n atmosphere of air were first described bli Rabin and Zimmerman (18) and IIartman et al. (9). The former authors established the amino acid and carbohydrate requirements and the latter established the vitamin and nitrogen base requirements. Hartman and Zimmerman (8) studied the inordinately large arginine requirement demonstrated by Rabin and Zimmerman (18) and found that, under the microaerobic conditions, the arginine dihydrolase enzyme system (10) limited proteinase biosynthesis as a result of the very rapid degradation of arginine. During this ~nvestigation, it was observed that aeration, as provided by the incubation of the cells in a shaken Warburg vessel with an atmosphere of air, inhibited proteinase forn~ation but did not inhibit the activity of preformed enzyme.The present investigation was undertalcell to define more fully the effects of oxygen and carbon dioxide on proteinase biosynthesis by ilonproliferating cells of S . faecalis var. liquejaciens in chemically defined media. Materials and MethodsThe organism used in this study was Streptococcnis jaecalis var. liquefaciens, strain 31, which was originally obtained from the Division of Bacteriology, Cornell University. Stoclc cultures were maintained a t -17 OC in litmus milk. Incubation temperature for all experiments was 37 OC. The basic medium was the optimal adaptation ~n e d i u~n (final >IS3/1 medium of Hartman et al. ( 9 ) ) .'This material was talccn from a thesis submitted by James F. Swiencicki in partial fulfillment of the requirements for a M.Sc. degree a t St. Bonaventure University.

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