Horse myoglobin

Isoelectric focusing of a mixture of proteins (1) soybean trypsin inhibitor (2) p-lactoglobulin A (3) p-iactoglobulin B (4) ovotransferrin (5) horse myoglobin (6) whale myoglobin and (7) cytochrome c. [Courtesy BioRaa Laboratories, Richmond, CA]... 

Enzymatic microreactors (7.5 nL) have been fabricated in the microfluidic chip to prepare the tryptic digest of equine (horse) myoglobin (14.2 pmol/p.L)... 

Lysozyme cytochrome c ribonuclease chymotrypsinogen horse myoglobin Open-tubular Fluorescence 15... 

Horse myoglobin P-lactoglobulin A P-lactoglobulin B swm, hca, bca Open-tubular UV 21... 

In a recent study, Hermans (1962) has indicated that only two of the three tyrosyl phenolic groups of myoglobin titrate below pH 13, this result being obtained for both whale and horse myoglobins. 

Angiotensin-I, methionine enkephalin, substance-P, bovine trypsin, horse cytochrome-C, horse myoglobin, bovine insulin and egg-white lysozyme were purchased from Sigma Chemical Co. (St. Louis, MO) and used without further purification. 

The use of tryptic peptides derived from related proteins, e.g., horse myoglobin in the analysis of human myoglobin, as IS in targeted quantitative analysis has been proposed as well [116]. 

Accuracy in MS depends on calibration of the mlz axis of the spectra. Calibration is typically performed using separate samples or solutions of the calibrant studied under identical instrumental conditions as the analyte. Calibrants are selected based on the ionization technique and the mlz range required for the analyte typical calibrants used for soft ionization methods with biomolecules include bovine trypsin fragments, bovine insulin (5734 Da), cytochrome c (12,361 Da), horse myoglobin (16,951 Da), lysozyme (14,317 Da), and propylene glycols. Separate solutions of the analyte prepared in the absence and presence of a calibrant species may also be used. Table 15.6 shows typical calibration peaks found with bovine trypsin autolysis fragments.15... 

In this context, the control of O2 affinity by the distal environment of the heme group in hemoproteins can be probed by comparison of wild-type compounds with mutants which do not contain distal histidine [105]. Replacement of distal histidine by glycine results in a 10-fold decrease in O2 affinity. Within the hemoproteins themselves, the lack of distal histidine in aplysia myoblobin compared to horse myoglobin increases the dissociation rate constant by a factor of six, whereas the association rate constants are identical for both systems. The data are again consistent with the stabilization of bound O2 via hydrogen-bonding in horse myoglobin. 

Table 1. Histidine residues in sperm whale and horse myoglobins...

Figure 8. Electropherogram of six protein standards obtained by capillary zone electrophoresis. The standards are A sperm whale myoglobin B horse myoglobin C human carbonic anhydrase D bovine carbonic anhydrase E 13-lactoglobulin B ...

Figure 3. The effect of separators on ultrathin-layer isoelectric focusing in rehydratable gels. Gels (120 jjim) containing 10% Dextran 35 plus 3% glycerol were rehydrated with 3% Servalyt pH 4-6 plus 5%, glycerol with the indicated concentration of different separators. On the left, a mixture of four marker proteins MYH-horse myoglobin, CAR-carbonic anhydrase, LAC-(3-lactoglobulin,...

The computer also played an enormously important part in protein crystallography at Cambridge. The elucidation ot the structure of horse myoglobin by Kendrew and his co-workers, announced in 1958, would not have been possible without EDSAC on which to process the 400 reflections measured. Subsequently EDSAC2 was used to produce a more refined structure based on 10,000 reflections and also to produce a determination of the structure of haemoglobin by Perutz and his co-workers. Both of these achievements were reported in Nature in... 

Finally we mention the natural abundance NMR spectra of carboxy sperm whale myoglobin, horse myoglobin and hemoglobin that have been determined by Conti and Paci (51). 

Figure 24. Gel electrofocusing according to Fawcett. Ampholine pH 7-10, anode at top. From left to right HbA, HbA+S, Hb A+C, whale myoglobin, horse myoglobin, mixture of whale and horse myoglobin, HbA. (Fawcett, FEBS Letters 31.)...

Figure 1 MIC of myoglobin mixture on siiica-bound Cu(il)-IDA. Column, 100 X 4.6 mm, 5-nm IDA-Vydac in Cu(ll) form 20 min linear gradient 0-100% B in A eluent A, 0.05 M acetic acid/MES/Hepes buffer, pH 8.0, containing 0.08 M Na2S04 and 2 x 10 M Cu(ll) eluent B, 0.05M acetic acid/MES/Hepes buffer, pH 5.5, containing 0.05M ammonium acetate and 2 x 10 M Cu(ll) flow rate, 1 mL/min temperature, 25"C. 1, Dog myoglobin 2, horse myoglobin 3, sperm whale myoglobin. (From Ref. 12.)...

Another method is to take the ratios of the peak heights of both spectra and to compare the results (Sec. 2.6.1.4). The ratios must be equal in the case of identical substances even if the concentrations are different (PPR method). This mathematical operation can be carried out by a short computer program. The printout is a set of data given in Table 4-7 for the comparison of trypsin and acetyltrypsin. Note that even small differences in the substances can easily be detected. In the fundamental spectra, the shape of the curves are very similar (Fig. 4-32 a) but the differences become clearly visible if the heights of the corresponding peaks in Fig. 4-32 b are mathematically manipulated. Other examples, such as the comparison of different varieties of beer [2], whale and horse myoglobin [25], and human and bovine hemoglobin [5] can be found in the cited literature. 

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