Properties of Inosine-5′-phosphate Dehydrogenase from Bacillus subtilis

1971 ◽  
Vol 49 (4) ◽  
pp. 473-475 ◽  
Author(s):  
Tai-Wing Wu ◽  
K. G. Scrimgeour
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Cooperative Interaction ◽  
Imp Dehydrogenase ◽  
Protein Subunits ◽  
Apparent Homogeneity ◽  
Complex Manner

Inosine-5′-phosphate (IMP) dehydrogenase has been purified to apparent homogeneity from extracts of Bacillus subtilis. The enzyme is inhibited by GMP in a complex manner which suggests cooperative interaction between protein subunits of IMP dehydrogenase. Several techniques have been used to desensitize the enzyme to inhibition by GMP. IMP dehydrogenase has a high molecular weight, and is composed of subunits each with a molecular weight of approximately 100 000. The properties of IMP dehydrogenase from B. subtilis are compatible with its being a regulatory enzyme in the biosynthesis of GMP from IMP.

Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Gel Filtration ◽  
Chain Structure ◽  
The Other ◽  
Single Chain ◽  
Apparent Homogeneity ◽  
Sequential Adsorption

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.

scholarly journals Chromatography of transforming deoxyribonucleic acid on methylated albumin and by gel filtration

1974 ◽  
Vol 137 (3) ◽  
pp. 543-546
Author(s):  
G. R. Barker ◽  
P. Hodges
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Deoxyribonucleic Acid ◽  
Degradation Products ◽  
Gel Filtration ◽  
Agarose Gel ◽  
Transforming Activity ◽  
Different Strains ◽  
Two Peaks

1. Native DNA from two strains of Bacillus subtilis was chromatographed by stepwise elution from MAK (methylated albumin on kieselguhr). 2. Transforming activity was confined to two out of the three main fractions, activity being distributed between the two peaks differently for DNA from the different strains. 3. Fractionation of DNA from both strains on 2% agarose gel gave two components. Approx. 75% of the material was eluted within the void volume of the column. Approx. 25% of the material consisted of degradation products of lower molecular weight. 4. Chromatography on MAK of the material of high molecular weight eluted from agarose gel gave a number of peaks differing in molecular weight, indicating that degradation of the DNA takes place during chromatography on MAK. 5. The distribution of transforming activity among the fractions from MAK suggests that degradation occurs preferentially in certain regions of the DNA.

scholarly journals Properties of the High-Molecular-Weight Deoxyribonuclease of Bacillus subtilis Degrading Single-Stranded DNA

1978 ◽  
Vol 84 (2) ◽  
pp. 533-539 ◽  
Author(s):  
Fabio COBIANCHI ◽  
Giovanni CIARROCCHI ◽  
Carmen ATTOLINI ◽  
Arturo FALASCHI
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Single Stranded Dna

scholarly journals Bacillus subtilis YhcR, a High-Molecular-Weight, Nonspecific Endonuclease with a Unique Domain Structure

2004 ◽  
Vol 186 (16) ◽  
pp. 5376-5383 ◽  
Author(s):  
Irina A. Oussenko ◽  
Roberto Sanchez ◽  
David H. Bechhofer
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Domain Structure ◽  
Micrococcal Nuclease ◽  
Structural Domain ◽  
Protein Extract ◽  
Triple Mutant ◽  
Rnase R ◽  
Unique Domain

ABSTRACT In a continuing effort to identify ribonucleases that may be involved in mRNA decay in Bacillus subtilis, fractionation of a protein extract from a triple-mutant strain that was missing three previously characterized 3′-to-5′ exoribonucleases (polynucleotide phosphorylase [PNPase], RNase R, and YhaM) was undertaken. These experiments revealed the presence of a high-molecular-weight nuclease encoded by the yhcR gene that was active in the presence of Ca2+ and Mn2+. YhcR is a sugar-nonspecific nuclease that cleaves endonucleolytically to yield nucleotide 3′-monophosphate products, similar to the well-characterized micrococcal nuclease of Staphylococcus aureus. YhcR appears to be located principally in the cell wall and is likely to be a substrate for a B. subtilis sortase. Zymogram analysis suggests that YhcR is the major Ca2+-activated nuclease of B. subtilis. In addition to having a unique overall domain structure, YhcR contains a hitherto unknown structural domain that we have named “NYD,” for “new YhcR domain.”

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