Ovalbumin molecular weight

The hemoglobin protein molecule (a tetramer with molecular weight of 68,000) and ovalbumin (molecular weight of 40,000) were found to remain as small clusters on the collapsed lipid tihn. " The presence of protein molecules is easily observed from the light shaded spots. The step heights... 

The elution volume, F/, and therefore the partition coefficient, is a function of the size of solute molecule, ie, hydrodynamic radius, and the porosity characteristics of the size-exclusion media. A protein of higher molecular weight is not necessarily larger than one of lower molecular weight. The hydrodynamic radii can be similar, as shown in Table 4 for ovalbumin and a-lactalbumin. The molecular weights of these proteins differ by 317% their radii differ by only 121% (53). 

FIGURE 4.29 Relation between molecular weight of lipoproteins and elution volume for combination GFC columns. Column 7.5 mm i.d. X 60 cm. Sample Chylomicron, VLDL, LDL, HDLj, HDL3, albumin, and ovalbumin. Elution 0.1 hA Tris—HCI buffer (pH 7.4). Flow rate 1.0 ml/min. 

FIGURE 8.12 Effect of pore diameter on SEC of standards (nondenaturin > mobile phase). Nondenaturing" refers to the effect on the stationary phase. Most iarge proteins were in fact denatured by this mobile phase (which was optimized for use with peptides, not proteins). Accordingly, it was necessary to use polyacrylamide to demonstrate the approximate range and position of Vo under these conditions. The polyacryiamide standards both eiuted at V with the 300-A coiumn (not shown). Columns and flow rate Same as in Fig. 8.11. Mobile phase Same as in Fig. 8.1. Sample key (B) Ovalbumin (43,000 Da) 0) polyacrylamide (1,000,000 Da) (K) polyacrylamide (400,000 IDa) (L) low molecular weight impurity in the polyacrylamide standards. Other samples as in Fig. 8.11. 

Figure 1. a - SDS-PAGE of fraction T (silver staining), lane 1 fraction T, lane 2 ovalbumine and lane 3 molecular weight standards. 

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...

Fig. 2.1. Semilogarithmic plot of molecular weight (Mr) of marker proteins vs relative mobility (Rf) of marker proteins in gels of different acrylamide concentrations %T. Proteins 1 aprotinin (6.5 kD) 2 lysozyme (14.5 kD) 3 soybean trypsin inhibitor (21.5 kD) 4 carbonic acid anhydrase (31 kD) 5 hen ovalbumin (45 kD) 6 bovine serum albumin (66 kD) 7 phosphorylase b (97.4 kD) 8 8-galactosidase (116 kD) 9 myosin (205 kD)...

Ovalbumin, a glycoprotein that is often present in standard molecular weight mixtures, gives a positive result with the Con A-HRP detection system. 

Figure B3.1.1 A 15% SDS-polyacrylamide gel stained with Coomassie brilliant blue. Protein samples were assayed for the purification of a proteinase, cathepsin L, from fish muscle according to the method of Seymour et al. (1994). Lane 1, purified cathepsin L after butyl-Sepharose chromatography. Lane 2, cathepsin L complex with a cystatin-like proteinase inhibitor after butyl-Sepharose chromatography. Lane 3, sarcoplasmic fish muscle extract after heat treatment and ammonium sulfate precipitation. Lane 4, sarcoplasmic fish muscle extract. Lanes M, low-molecular-weight standards aprotinin (Mr 6,500), a-lactalbumin (Mr 14,200), trypsin inhibitor (Mr 20,000), trypsinogen (Mr 24,000), carbonic anhydrase (Mr 29,000), gylceraldehyde-3-phosphate dehydrogenase (Mr 36,000), ovalbumin (Mr 45,000), and albumin (Mr 66,000) in order shown from bottom of gel. Lane 1 contains 4 pg protein lanes 2 to 4 each contain 7 pg protein.

Power supply and electrophoresis apparatus Protein molecular weight standards (suggested standards phosphorylase [97,400 Da], bovine serum albumin [66,200 Da], ovalbumin [45,000 Da], carbonic an-hydrase [31,000 Da], soybean trypsin inhibitor [21,500 Da], and lysozyme [14,400 Da] at 1 mg/ml each in a single mixture)... 

Figure 1. SDS-PAGG analysis of alkaline-dissolved Bacillus thuringiensis subspecies kurstaki (BTK) and israelensis (BTI) -endotoxin at 25 yg per track (1) BTK -endotoxin from Biochem Products - US Division (Salsbury Labs., Inc.), (2) BTI 6-endotoxin from Sandoz Inc., (3) BTI (Sandoz) -endotoxin purified by DEAE-anion exchange chromatography, (4) percipitate formed after dialysis of BTI (Sandoz) -endotoxin into pH 4.5 sodium acetate buffer, (5) soluble fraction after dialysis of BTI (Sandoz) -endotoxin into pH 4.5 sodium acetate buffer, (6) BTI (Sandoz) -endotoxin purified by Sephadex G-75 gel filtration chromatography at Rf 1.35, (7) at Rf 1.58, and (8) BTI strain IFC-1 -endotoxin from Biochem Products - US Division (Salsbury Labs., Inc.). S, molecular weights as indicated X1000 for bovine serum albumin (BSA), ovalbumin (OA), trypsin, and myoglobin. Reproduced with permission from Ref. 29. Copyright 1984, Academic Press, Inc.

Figure 5. SDS-Page analysis of alkaline-dissolved Bacillus thuringiensis israelensis (BTI) 6-endotoxin from Sandoz Inc. at 25 yg per track (1) BTI 6-endotoxin as prepared in Figure 1 (Track 2), (2) soluble fraction after dialysis of BTI 6-endotoxin into pH 4.5 sodium acetate buffer, and (3) 25K component from BTI 6-endotoxin after pH 4.5 percipitation and DEAE-anion exchange chromatography. S, molecular weight markers from top to bottom bovine serum albumin (68K daltons), ovalbumin (43K), and myoglobin (16K).

Figure 11.1 Native polyacrylamide gel (5%) electrophoresis of purified fructosyltransferase. (a) Lane 1, molecular weight markers (45 kDa ovalbumin, 67kDa bovine serum albumin (BSA), and 134kDa BSA dimer) lane 2, pure fructosyltransferase. (b) Pure fructosyltransferase (one lane from the same gel was cut and stained for fructosyltransferase activity).

Figure 2. SDS gel electrophoresis of the products of partial cystine cleavage for several test proteins. A. molecular weight standards, B. yeast alcohol dehydrogenase. C. P-lactoglobulin, D. hen egg lysozyme, E. ovalbumin, F. calf fetal serum fetuin. Molecular weight standards are indicated by arrows on the left side of the gel and are bovine serum albumin (66,300), bovine liver glutamate dehydrogenase (55,400), porcine muscle lactate ddiydiogenase (36,500), bovine erythrocyte carbonic anhydrase (31,000), soybean trypsin inhibitor (21,500), hen egg lysozyme (14,400), bovine lung aprotinin (6,000), unresolved bovine pancreatic insulin A and B chains.

If the molecular weights of pepsin and pepsinogen are 35,000 and 38,000, respectively (61), each of these molecules contains one atom of phosphorus (28, 60). Since it had been shown that ovalbumin and a-casein are readily dephosphorylated by certain phosphatases from mammalian tissue, and from potato, the action of these enzymes on pepsin and its precursor w as studied. It was found that only the potato phosphatase at pH 5.6 de-phosphorylates pepsin and pepsinogen, whereas prostate phosphatase does not act on these proteins. The intestinal enzyme, although not active at pH 6.0, liberates phosphorus at pH 8.9 (67). 

Materials. The CMC was a commercial sample supplied by Hercules Inc. (Wilmington, DE) of average molecular weight 250,000 Da and a degree of substitution of 1.2. Lysozyme and ovalbumin were from Sigma Chemicals (St. Louis, MO). 

Glycoproteins substances of high molecular weight having many of the physical properties of a protein, but containing covalently bonded carbohydrate component s) mucoproteins, mucosubstances, mucins ovalbumin, thyroglobulin, ceruloplasmin... 

For an investigation of the capability of macromolecules to diffuse through the membranes, we used six test proteins ranging in molecular weight from 17000 to 80 000 Da myoglobin (MYO, 17000 Da) soybean trypsin inhibitor (STI, 20 000 Da) carbonic anhydrase (CAR, 29 000 Da) ovalbumin (OVA, 45 000 Da) bovine serum albumin (ALB, 66000 Da) and human transferrin (TFN, 80000 Da). 

FIGURE 7. Determination of the molecular weight of the purified PSPBP from Acanthocardia tuberculatum foot by gel electrophoresis on denaturing conditions. Molecular weight marker proteins were commercial myosine (205 kDa), P-galactosidase (116 kDa), phosphorylase B (97.4 kDa), albumin (66 kDa), ovalbumin (45 kDa) and carbonic anhydrase (29 kDa). The plot represents the relative mobilities of proteins vs. Log (Molecular Weight). 

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