scholarly journals Myelin basic proteins in myelin subfractions from normal and quaking mice

1979 ◽  
Vol 183 (1) ◽  
pp. 159-162
Author(s):  
G E Fagg ◽  
T V Waehneldt
Keyword(s):  
Distribution Pattern ◽  
Basic Protein ◽  
Littermate Control ◽  
Basic Proteins ◽  
Myelin Subfractions ◽  
And Control ◽  
Quaking Mice

The relative proportions of four myelin basic proteins (preL, L, preS,S) were determined in myelin subfractions prepared from the forebrains of quaking and littermate control mice. The distribution pattern of each protein was similar in both mutant and control fractions. The S component was the only basic protein present in low amounts in myelin from the mutant.

Changes in protein spectra of bean seed during germination

1970 ◽  
Vol 48 (7) ◽  
pp. 1347-1350 ◽  
Author(s):  
Pei-Show Juo ◽  
G. Stotzky
Keyword(s):  
Acetic Acid ◽  
Phaseolus Vulgaris ◽  
Basic Protein ◽  
The Other ◽  
Globulin Fraction ◽  
Bean Seed ◽  
Basic Proteins ◽  
Number Of Components ◽  
Red Kidney Bean ◽  
Protein Spectra

Globulins, albumins, and basic proteins were extracted from seeds of red kidney bean (Phaseolus vulgaris), and their distribution was in a ratio of about 3:2:1, respectively. The globulin fraction constituted a major portion of the reserve proteins and was hydrolyzed rapidly during germination. More than 90% of the basic proteins, extractable with 0.05 N acetic acid, disappeared 12 days after germination. Although the decrease in total albumin was not as marked as with the other two fractions, a number of components of this fraction disappeared during the early stages of germination, but several new components were detected about 8 days after germination. The apparent synthesis of new globulin components during germination was also observed, but no synthesis of basic protein could be detected.

scholarly journals Proteolytic and peroxidatic reactions of commercial horseradish peroxidase with myelin basic protein

1978 ◽  
Vol 169 (3) ◽  
pp. 567-575 ◽  
Author(s):  
Wendy Cammer ◽  
Lesley Z. Bieler ◽  
William T. Norton
Keyword(s):  
Horseradish Peroxidase ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein A ◽  
Low Molecular Weight ◽  
Basic Proteins ◽  
Molecular Weights ◽  
Low Concentrations ◽  
High Concentrations ◽  
A Minor

Degradation of myelin basic protein during incubations with high concentrations of horseradish peroxidase has been demonstrated [Johnson & Cammer (1977) J. Histochem. Cytochem.25, 329–336]. Possible mechanisms for the interaction of the basic protein with peroxidase were investigated in the present study. Because the peroxidase samples previously observed to degrade basic protein were mixtures of isoenzymes, commercial preparations of the separated isoenzymes were tested, and all three degraded basic protein, but to various extents. Three other basic proteins, P2 protein from peripheral nerve myelin, lysozyme and cytochrome c, were not degraded by horseradish peroxidase under the same conditions. Inhibitor studies suggested a minor peroxidatic component in the reaction. Therefore the peroxidatic reaction with basic protein was studied by using low concentrations of peroxidase along with H2O2. Horseradish peroxidase plus H2O2 caused the destruction of basic protein, a reaction inhibited by cyanide, azide, ferrocyanide, tyrosine, di-iodotyrosine and catalase. Lactoperoxidase plus H2O2 and myoglobin plus H2O2 were also effective in destroying the myelin basic protein. Low concentrations of horseradish peroxidase plus H2O2 were not active against other basic proteins, but did destroy casein and fibrinogen. Although high concentrations of peroxidase alone degraded basic protein to low-molecular-weight products, suggesting the operation of a proteolytic enzyme contaminant in the absence of H2O2, incubations with catalytic concentrations of peroxidase in the presence of H2O2 converted basic protein into products with high molecular weights. Our data suggest a mechanism for the latter, peroxidatic, reaction where polymers would form by linking the tyrosine side chains in basic-protein molecules. These data show that the myelin basic protein is unusually susceptible to peroxidatic reactions.

Cytoplasmic DNA and basic protein synthesis in Megalobatrachus davidianus oocytes

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 271-283
Author(s):  
Y. C. Kong ◽  
I. F. Lau ◽  
W. L. Lam ◽  
C. M. Choy
Keyword(s):  
Protein Synthesis ◽  
Dna Synthesis ◽  
Dose Response ◽  
Dna Content ◽  
Active Site ◽  
Basic Protein ◽  
Basic Proteins ◽  
Biochemical Event ◽  
Cytoplasmic Dna

Mature Megalobatrachus oocytes contain 43 µg DNA per oocyte, as compared with 250 pg DNA in a hepatocyte of the same animal. Megalobatrachus oocytes respond to CdR treatment by an increased incorporation of [3H]lysine into basic proteins associated with ooplasmic particles, with an optimal CdR concentration at 2 mM. The nucleolus is the most active site of [3H]lysine incorporation. It is suggested that CdR-stimulated basic protein synthesis is a common biochemical event during amphibian oogenesis. The dose response to CdR treatment may be a function of the c-DNA content or c-DNA synthesis potential in the ooplasm.

PSX-A-3 Late-Breaking: Analysis of serum chemistry for metabolic function in GnRH-II receptor knockdown and littermate control boars

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 377-377
Author(s):  
Caitlin E Ross ◽  
Amy T Desaulniers ◽  
Rebecca A Cederberg ◽  
Ginger A Mills ◽  
Clay A Lents ◽  
...  
Keyword(s):  
Equal Opportunity ◽  
Physiological Role ◽  
Lactic Dehydrogenase ◽  
High Density Lipoproteins ◽  
Mrna Levels ◽  
Gamma Glutamyl Transpeptidase ◽  
Littermate Control ◽  
Elevated Creatinine ◽  
Metabolic Disruption ◽  
And Control

Abstract Pigs are the only livestock species encoding functional proteins for both the second form of gonadotropin-releasing hormone (GnRH-II) and its receptor (GnRHR-II), which are uniquely expressed in reproductive and non-reproductive tissues. To examine the physiological role of the GnRH-II/GnRHR-II system, we produced a swine line with reduced endogenous levels of GnRHR-II (GnRHR-II KD); males exhibit 70% diminished testicular GnRHR-II mRNA levels and 82% reduced circulating testosterone concentrations. Given that testosterone impacts metabolism, blood was collected from GnRHR-II KD (n = 5) and littermate control (n = 5) boars via indwelling jugular catheters, with serum isolated and subjected to veterinary diagnostic panels for metabolic analyte examination (PhysLab, Lincoln, NE). Statistical analyses utilized the MIXED procedure of SAS; the model included line as fixed and litter as random effects. Creatine kinase and blood urea nitrogen (BUN):creatinine ratios were elevated, creatinine was reduced (P < 0.01), and thyroxine tended to be decreased (P < 0.10) in GnRHR-II KD compared with control boars. Glucose, BUN, amylase, and lipase levels were not different. Liver products differed in transgenic versus control boars; levels of lactic dehydrogenase, aspartate and alanine aminotransferases (AST; ALT), and gamma-glutamyl transpeptidase were higher, whereas AST:ALT ratios, total protein, albumin, and globulin levels were lower (P < 0.05) in GnRHR-II KD boars. Albumin:globulin ratios and bilirubin (total and direct) did not differ. Additionally, serum cholesterol was decreased (P < 0.05), non-high density lipoproteins (HDLs) and low density lipoproteins (LDLs) tended to be decreased (P < 0.10), and triglycerides, HDLs, and cholesterol:HDL ratios did not differ between GnRHR-II KD and control males. These data suggest metabolic disruption in GnRHR-II KD boars, which may be due to suppressed gonadal steroidogenesis or ubiquitous knockdown of GnRHR-II expression. Supported by USDA/NIFA AFRI (2017-67015-26508) and Hatch Multistate (NEB-26–244) funds. USDA is an equal opportunity provider and employer.

scholarly journals STUDIES OF THE TRANSMISSIBLE AGENT OF THE ROUS CHICKEN SARCOMA I

1940 ◽  
Vol 72 (6) ◽  
pp. 697-705 ◽  
Author(s):  
David Shemin ◽  
E. E. Sproul ◽  
James W. Jobling
Keyword(s):  
Basic Protein ◽  
Active Agent ◽  
Basic Proteins ◽  
Rous Sarcoma

The viscosity of Rous sarcoma extracts can be reduced with a polysaccharide enzyme isolated from pneumococcus or testis without destruction of the active agent and thus more concentrated active filtrates can be obtained. The active agent can be precipitated with basic proteins. The basic protein can be separated from the components originally coming from the tumor filtrate by electrophoresis.

Two-dimensional gel electrophoresis of human brain proteins. V. Non-equilibrium gel electrophoresis, with detection of a myelin basic protein mutation--MBL-Duarte.

1982 ◽  
Vol 28 (4) ◽  
pp. 813-818 ◽  
Author(s):  
D E Comings ◽  
A Pekkula-Flagan
Keyword(s):  
Human Brain ◽  
Myelin Basic Protein ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Myelin Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Brain Proteins ◽  
Basic Proteins ◽  
A Charge ◽  
Non Equilibrium

Abstract To examine the basic human brain proteins, we subjected 9 mmol/L urea extracts to non-equilibrium gel electrophoresis. The pattern observed differs distinctly from that with equilibrium gel electrophoresis. With this technique, the myelin proteins (myelin basic protein, proteolipids, and basic Wolfgram proteins) and many other unindentified major basic proteins can be demonstrated. The myelin basic proteins occur as two major polypeptides of different charge and slightly different molecular mass, indicating the action of at least two genes. The proteolipid proteins occur as a long series of charge isomers, suggesting multiple genes or extensive post-transcriptional modification. In one patient with schizophrenia, a charge-change mutation of the larger myelin basic protein (MBL) was observed and is termed "MBL-Duarte."

Sign in / Sign up

Export Citation Format

Share Document