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Cyanogen bromide fragments

With the use of oligonucleotide probes based on the amino acid sequences of these protease V8-obtained peptides and of cyanogen bromide fragments of the porcine H,K-ATPase P subunit, cDNA clones for the rat [12,25] and rabbit [74] H,K-ATPase P subunit were then isolated. [Pg.32]

Extensive analysis of cyanogen bromide fragmented peptides of type I, III, and V collagens by MALDI-MS has shown that type V collagen from bovine skin is highly glycosylated, while type I and III collagens contain... [Pg.499]

Bl. Baker, H. N., Jackson, R. L., and Gotto, A. M., Cyanogen bromide fragments of the human plasma high density, apoLP-Gln-I Isolation of a helical peptide. Circulation 24, Suppl. II, 255 (1972). Abstr. [Pg.144]

Residues 30 and 31, glutamine and proline, respectively (27), were originally assigned in the reversed order on the basis of partial removal of residue (homoserine) from cyanogen bromide fragment [27-32] by carboxypeptidase A (26). The action of the latter is generally as-... [Pg.181]

The reconstructed total ionization chromatogram of the trimethylsily-lated polyamino alcohols, prepared by the outlined procedure, from the acid hydrolysis of the C-terminal cyanogen bromide fragment of actin is shown in Figure 1.14 [51]. The identification of the peaks was achieved by... [Pg.43]

Figure 1.15. Oligopeptides identified by GC-MS-computer as their O TMS polyamino alcohol derivatives from acid hydrolysate of C terminal cyanogen bromide fragment of actin. The reassembled eicosapeptide is shown (A) (reproduced from [51])... Figure 1.15. Oligopeptides identified by GC-MS-computer as their O TMS polyamino alcohol derivatives from acid hydrolysate of C terminal cyanogen bromide fragment of actin. The reassembled eicosapeptide is shown (A) (reproduced from [51])...
Syska et al (1976) showed that the cyanogen bromide fragment CN4 (residues 96-116) had 75% of the inhibitory action of troponin I. A larger fragment, CFl (residues 64-135), which contained the CN4 sequence, also showed the inhibitory action but to a lesser extent than the CN4 fragment. The inhibition was also neutralized by troponin C. [Pg.10]

W2. Wiman, B., and Wallen, P. M., Amino-acid sequence of the cyanogen-bromide fragment from human plasminogen that forms the linkage between the plasmin chains. Eur. J. Biochem. 58, 539-547 (1975). [Pg.168]

The sequence of stem bromelain contains one sulfhydryl group and three intrapeptide disulfide bonds [45]. The homology between stem bromelain and members of the papain family was first demonstrated by alignment of cyanogen bromide fragments of stem bromelain with the sequence of papain [48,54] and by studying the immunological cross-reactions between different cysteine proteinases [55-57]. [Pg.138]

K. Goto, T. Murachi, and N. Takahashi. Structural studies on stem bromelain isolation, characterization and alignment of the cyanogen bromide fragments. FEBS Lett. 62 93 (1976). [Pg.149]

Morrison, J. R., et al. (1990). Studies on the Formation, Separation and Characterization of Cyanogen Bromide Fragments of Human Al Apolipoprotein, Biochem. 186 152-154. [Pg.183]

Other Studies of Heme Proteins. Monzani et al. have used H relaxometry to study Mn(III)-substituted heme complexes with cyanogen bromide fragments of human serum albumin. [Pg.577]

Figure 2. "Western blot" analysis of a timecourse of treatment of the isolated 15.7 kDa cyanogen bromide fragment with Sigma carboxypeptidase Y in the presence of 5 mM PMSF. Shown is the immunoblot after probing with FAC2. Lane A, 0 min incubation, no ensyme lane B, 0 min + enzyme lane C, 15 min + enzyme lane D, 30 min + enzyme and, lane E, 60 min + enzyme. Figure 2. "Western blot" analysis of a timecourse of treatment of the isolated 15.7 kDa cyanogen bromide fragment with Sigma carboxypeptidase Y in the presence of 5 mM PMSF. Shown is the immunoblot after probing with FAC2. Lane A, 0 min incubation, no ensyme lane B, 0 min + enzyme lane C, 15 min + enzyme lane D, 30 min + enzyme and, lane E, 60 min + enzyme.
TABLE I. Predicted Cyanogen Bromide Fragments from the Spinach psbB Gene Product (CPa-1) and Sequcncesof Isolated Peptides Bearing the Epitope of the Monoclonal Antibody FAC2. [Pg.641]

Figure 2. Amino-terminal amino acid sequences of the barley aminotransferase and of the internal cyanogen bromide fragment Also given are the oligonucleotide primers used for the polymerase chain reaction... Figure 2. Amino-terminal amino acid sequences of the barley aminotransferase and of the internal cyanogen bromide fragment Also given are the oligonucleotide primers used for the polymerase chain reaction...
Cyanogen bromide fragments (rat tail tendon— types I and ID) CNBr fragments (rat tail tendon— types I and III)... [Pg.469]

D and E are related, since their cyanogen bromide fragmentation patterns or tryptic fingerprints were similar (19> 29). From... [Pg.132]

Is there a trp-phe sequence or a phe-phe sequence in either of the cyanogen bromide fragments There is a phe-phe sequence in E and that fragment also contains trp as its N-terminus. In addition, A is known to contain trp as its C-terminus and B contains ala as its N-terminus. From fragment E, the... [Pg.1400]

Figure 6 Ideal SEC of myoglobin fragments and a mixture of synthetic peptide standards. Column same as Fig. 2. Mobile phase 50 mM KH2P04, containing 500 mM KCI and 8M urea, pH 6.5 flow rate, 0.2mL/min temperature, 26 C. (A) Elution profile of horse heart myoglobin (Mb) and its cyanogen bromide cleavage fragments (I, II, I + II, III) (B) elution profile of horse heart Mb and synthetic peptide standards 1-5 (sequences of standards are shown in Table 1) (C) plot of log,o MW versus elution time of Mb, cyanogen bromide fragments of Mb, and the five synthetic peptide standards. (From Ref. 37.)... Figure 6 Ideal SEC of myoglobin fragments and a mixture of synthetic peptide standards. Column same as Fig. 2. Mobile phase 50 mM KH2P04, containing 500 mM KCI and 8M urea, pH 6.5 flow rate, 0.2mL/min temperature, 26 C. (A) Elution profile of horse heart myoglobin (Mb) and its cyanogen bromide cleavage fragments (I, II, I + II, III) (B) elution profile of horse heart Mb and synthetic peptide standards 1-5 (sequences of standards are shown in Table 1) (C) plot of log,o MW versus elution time of Mb, cyanogen bromide fragments of Mb, and the five synthetic peptide standards. (From Ref. 37.)...

See other pages where Cyanogen bromide fragments is mentioned: [Pg.510]    [Pg.393]    [Pg.181]    [Pg.182]    [Pg.307]    [Pg.326]    [Pg.81]    [Pg.82]    [Pg.149]    [Pg.272]    [Pg.222]    [Pg.291]    [Pg.44]    [Pg.270]    [Pg.271]    [Pg.274]    [Pg.13]    [Pg.37]    [Pg.245]    [Pg.13]    [Pg.304]    [Pg.641]    [Pg.641]    [Pg.2475]    [Pg.114]    [Pg.132]    [Pg.133]    [Pg.133]    [Pg.138]    [Pg.445]    [Pg.449]   
See also in sourсe #XX -- [ Pg.291 , Pg.292 ]




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