scholarly journals Structural genes for phosphatases inAspergillus nidulans

1986 ◽  
Vol 47 (2) ◽  
pp. 83-91 ◽  
Author(s):  
Mark X. Caddick ◽  
Herbert N. Arst
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Aspergillus Nidulans ◽  
Structural Gene ◽  
Essential Role ◽  
Thermal Inactivation ◽  
Sufficient Conditions ◽  
Structural Genes ◽  
Electrophoretic Patterns ◽  
Staining Techniques

SUMMARYAlthough the fungusAspergillus nidulanshas a multiplicity of phosphatases and of genes where mutations affect one or more phosphatases, we have succeeded in identifying structural genes for three phosphatases as well as one other gene which might encode a fourth. Using both conditional and non-conditional mutations,palD has been shown to be the structural gene for a phosphate-repressible alkaline phosphatase,palG to be the structural gene for a non-repressible alkaline phosphatase which apparently exists in two electrophoretically distinct forms (but whose rates of thermal inactivation are apparently very similar) andpacA to be the structural gene for both intracellular and secreted forms of a phosphate-repressible acid phosphatase. Colony staining techniques for the enzymes specified bypalD andpacA have been described previously but we have now shown that the enzyme specified bypalG can be detected by staining toluene-permeabilized colonies. Mutations inpacG lead to loss of non-repressible acid phosphatase as judged by colony staining and electrophoretic patterns but their effects on assays of activity in cell-free extracts are only marginal. Under phosphate-limited, but not phosphate-starved or phosphate-sufficient, conditions,pacG−mutations also affect the regulation of other, phosphate-repressible phosphatases. None of these phosphatases, alone or in combination, plays an essential role.

scholarly journals REGULATION OF PHOSPHATE METABOLISM IN NEUROSPORA CRASSA: IDENTIFICATION OF THE STRUCTURAL GENE FOR REPRESSIBLE ACID PHOSPHATASE

Genetics ◽  
1976 ◽  
Vol 84 (2) ◽  
pp. 183-192
Author(s):  
Robert E Nelson ◽  
John F Lehman ◽  
Robert L Metzenberg
Keyword(s):  
Acid Phosphatase ◽  
Neurospora Crassa ◽  
Structural Gene ◽  
Group Iv ◽  
Structural Genes ◽  
Wild Type ◽  
Linkage Groups ◽  
Michaelis Constant ◽  
The Right

ABSTRACT A mutant of Neurospora crassa with an altered repressible acid phosphatase has been isolated. The enzyme is much more thermolabile than that of wild type, and has an increased Michaelis constant. Tests of allelic interactions (in partial diploids) and in vitro mixing experiments were consistent with the mutation being in the structural gene for the enzyme. This gene, pho-3, was found to be located in the right arm of Linkage Group IV (LG IV). Thus, pho-3 and the structural gene for repressible alkaline phosphatase, pho-2 (LG V), map in separate linkage groups and cannot be part of the same operon. Neither of these structural genes is linked to the known regulatory genes, nuc-1 (LG I), nuc-2 (LG II), and preg (LG II).

scholarly journals Genetic analysis of the phosphatases in Aspergillus nidulans

1965 ◽  
Vol 6 (1) ◽  
pp. 13-26 ◽  
Author(s):  
G. Dorn
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Genetic Analysis ◽  
Aspergillus Nidulans ◽  
Alkaline Ph ◽  
Wild Type ◽  
Linkage Groups ◽  
Partial Restoration ◽  
Suppressor Mutations ◽  
Alkaline And Acid Phosphatase

Summary1. A histochemical method has been applied to the detection of alkaline and acid phosphatase mutants in single colonies of Aspergillus nidulans.2. With the above method it has been possible to isolate mutants in which the alkaline and acid phosphatase activities are affected either separately or simultaneously.3. Crude extracts of wild-type A. nidulans contain four electrophoretically distinct phosphatase components, two with activity at alkaline pH and two with activity at acid pH. Genes affecting three of the four components have been identified.4. Two suppressor mutants of an alkaline phosphataseless mutant (palB7) have been isolated. In a strain carrying palB7 and one of these suppressors, the restoration of an alkaline phosphatase component is accompanied by loss of the faster acid phosphatase component. In a similar strain carrying the other suppressor, the partial restoration of the alkaline phosphatase component goes with an electrophoretic alteration of the slower acid phosphatase component.5. Genetic analysis of twenty-seven mutants has resulted in the identification of fifteen loci affecting the phosphatases. All these loci have been assigned to linkage groups, and twelve of them were also mapped meiotically in relation to other loci.6. One possible model (based on heteropolymeric proteins) has been proposed to account for the electrophoretic and genetic data on the various phosphatase and suppressor mutations.

scholarly journals Use of isozymes as chromosome markers in wheat-rye addition lines and in triticale

1975 ◽  
Vol 26 (2) ◽  
pp. 187-201 ◽  
Author(s):  
K. S. Tang ◽  
G. E. Hart
Keyword(s):  
Acid Phosphatase ◽  
Alcohol Dehydrogenase ◽  
Structural Gene ◽  
Spring Wheat ◽  
Chinese Spring ◽  
Addition Lines ◽  
Structural Genes ◽  
Glutamate Oxaloacetate Transaminase ◽  
Chinese Spring Wheat ◽  
Adh Genes

SUMMARYThe alcohol dehydrogenase (ADH), glutamate oxaloacetate transaminase (GOT), acid phosphatase (ACPH), endopeptidase (EP) and aminopeptidase (AMP) zymogram phenotypes of Chinese Spring wheat, Imperial rye, the Chinese Spring-Imperial triticale and the series of seven disomic Imperial chromosome additions to Chinese Spring were determined. It was found that the zymogram phenotypes produced for one or more of the enzymes by each of the Imperial chromosomes 3, 6, C and D differ sufficiently from that of Chinese Spring so as to provide evidence for the presence or absence of each of these chromosomes in addition lines and triticales. The structural genes Got-R2 and Got-R3 were located in Imperial chromosomes 6 and 3 respectively and other genes involved in the production of GOT in chromosomes C and D. By analysis of GOT alone, evidence for the presence or absence of Imperial chromosomes 3, 6, C and D in addition lines and triticales can be obtained. Adh-R1 was located in chromosome C and a gene(s) involved in the production of an ACPH was located in chromosome D.The linkages obtained for Got-R2, Got-R3 and Adh-R1 demonstrate homoeology between the Imperial chromosomes 3, 6 and C and the Chinese Spring chromosomes of groups 3, 6 and 4 respectively. The discovery that Adh-R1 is located in Imperial chromosome C also suggests that the 4R/7R and 7R/4R homoeologous groupings proposed elsewhere for the chromosomes of the rye cultivars Imperial, Dakold, and King II should be reassessed, since they are inconsistent with the known linkages of Adh-R1 in the three cultivars. The finding in King II of two forms of ADH and of two ADH genes has been reported. The results of our study of Imperial, King II, and Dakold indicate that rye possesses but one ADH and only one ADH structural gene.

Effects of Kanwa on Rat Gastrointestinal Phosphatases

2010 ◽  
Vol 3 (3) ◽  
pp. 1147-1152
Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Acid Phosphatase ◽  
Sodium Carbonate ◽  
Elevated Level ◽  
Food Additive ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Diagnostic Indices ◽  
High Level

This study investigates the effects of kanwa on rat gastrointestinal phosphatases. The rats were administered 7% w/v concentration of  trona (Kanwa) orally for a period of two weeks in order to investigate how this compound is being used as food additive in some homes in Nigeria. The Kanwa used in this study was the handpicked variety obtained from sellers from Anyigba market in eastern part of Kogi State, Nigeria. Kanwa, a hydrated sodium carbonate (Na2CO3NaHCO3.2H2O) was obtained as a dried lake salt. Acid phosphatase has the ability to dephosphorylate molecules containing phosphate group. The decreased and elevated level in serum or plasma acid and alkaline phosphatases serves as diagnostic indices for various diseases. Results showed that there was increase and decrease of acid phosphatase (ACP) activities in both the stomach and small intestine. The activities of alkaline phosphatase (ALP) fluctuated in the small intestine. However, in the stomach, an increase activity of ALP was noticed throughout the period of ‘Kanwa’ administration. We concluded that although the level of ‘Kanwa’ consumed in most homes may not be toxic if not taken continuously or repeatedly. Thus, continuous consumption should be discouraged as accumulation of high level of ‘Kanwa’ may cause damages or injuries to the various organs/tissues and may disrupt normal body function.

scholarly journals Bone-Derived Serum Enzymes and Bone Density in Perimenopausal Caucasian Women

1993 ◽  
Vol 30 (2) ◽  
pp. 191-194 ◽  
Author(s):  
J D Johnston ◽  
S Koneru ◽  
T Kuwana ◽  
S B Rosalki
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Bone Density ◽  
Femoral Neck ◽  
Serum Levels ◽  
Bone Alkaline Phosphatase ◽  
Serum Enzymes ◽  
Tartrate Resistant Acid Phosphatase ◽  
Vertebral Bone ◽  
Caucasian Women

Serum levels of bone-origin alkaline phosphatase and of tartrate-resistant acid phosphatase were measured in Caucasian women aged 41–69 years who had volunteered for bone densitometry. Bone alkaline phosphatase and tartrate-resistant acid phosphatase were inversely correlated with vertebral bone density and with femoral neck bone density. Bone alkaline phosphatase and acid phosphatase were also significantly correlated, consistent with the concept of ‘coupling’ between osteoblast and osteoclast activity.

scholarly journals Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture

1972 ◽  
Vol 127 (1) ◽  
pp. 87-96 ◽  
Author(s):  
P. G. Bolton ◽  
A. C. R. Dean
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Continuous Culture ◽  
Activity Profile ◽  
Glucose Effect ◽  
Ph Values ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Phosphatase synthesis was studied in Klebsiella aerogenes grown in a wide range of continuous-culture systems. 2. Maximum acid phosphatase synthesis was associated with nutrient-limited, particularly carbohydrate-limited, growth at a relatively low rate, glucose-limited cells exhibiting the highest activity. Compared with glucose as the carbon-limiting growth material, other sugars not only altered the activity but also changed the pH–activity profile of the enzyme(s). 3. The affinity of the acid phosphatase in glucose-limited cells towards p-nitrophenyl phosphate (Km 0.25–0.43mm) was similar to that of staphylococcal acid phosphatase but was ten times greater than that of the Escherichia coli enzyme. 4. PO43−-limitation derepressed alkaline phosphatase synthesis but the amounts of activity were largely independent of the carbon source used for growth. 5. The enzymes were further differentiated by the effect of adding inhibitors (F−, PO43−) and sugars to the reaction mixture during the assays. In particular, it was shown that adding glucose, but not other sugars, stimulated the rate of hydrolysis of p-nitrophenyl phosphate by the acid phosphatase in carbohydrate-limited cells at low pH values (<4.6) but inhibited it at high pH values (>4.6). Alkaline phosphatase activity was unaffected. 6. The function of phosphatases in general is discussed and possible mechanisms for the glucose effect are outlined.

SIGNIFICANCE OF TRANSAMINASE ACTIVITY OF SERUM

PEDIATRICS ◽  
1959 ◽  
Vol 24 (3) ◽  
pp. 360-361
Author(s):  
SAMUEL P. BESSMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Transaminase Activity ◽  
Specific Approach ◽  
Normal Tissues ◽  
The Past ◽  
Glycolytic Activity ◽  
Enzyme Characteristic ◽  
Phosphatase Alkaline

THE MEASUREMENT of enzyme activity of serum as an indicator of disease has a long history in medicine. In the past, it has been the aim of the designers of these methods to make them as specific as possible for assay of an enzyme characteristic of a particular system or group of similar organs. Examples of these venerable tests are those for amylase, acid phosphatase, alkaline phosphatase and choline esterase in the serum. Warburg made the first departure from this specificity by demonstrating that the activity of triosephosphate dehydrogenase in the serum of animals with cancer was much greater than that of controls. This test was partially specific, for as Warburg had earlier shown, the glycolytic activity of tumors is much greater than that of normal tissues. The non-specific approach became extreme with the introduction of the measurement of the glutamic-oxalacetic transaminase reaction in the diagnosis of acute coronary disease.

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