ライフサイエンスコーパス: CNBr

1 CNBr C-terminal analysis showed that the inactive HIC pe

2 CNBr cleavage analysis of Fes isolated from 32PO4-labele

3 CNBr cleavage at amino acid 330 produced a monomer-sized

4 CNBr cleavage at the single methionine in the connecting

5 CNBr cleavage of recombinant receptors expressed in COS-

6 CNBr cleavage of the broad approximately 80-kDa complex

7 CNBr digestion of [(3)H]7-(benzoyldihydrocinnamoyl)Taxol

8 CNBr digestion of both photolabeled P-glycoproteins gave

9 CNBr digestion of complexes formed with two additional r

10 CNBr digestion of the 50-kDa component resulted in an in

11 CNBr digestion of the protein preparations followed by M

12 CNBr digestion, followed by trypsin and then proteinase

13 CNBr fragmentation of the receptor protein, used for the

14 CNBr hydrolysis of [125I]RTI 82-labeled rat striatal and

15 CNBr peptide profiles of the S-layer proteins from C. re

16 ognize a conformational epitope present in a CNBr digestion fraction of lactoferrin.

17 be derived from the amino acid sequence of a CNBr fragment of the purified receptor.

18 ate-polyacrylamide gel electrophoresis after CNBr cleavage of the labeled protein.

19 etermined using the peptides generated after CNBr digestion of the purified enzyme.

20 The heme-peptide adducts isolated after CNBr/lysylendopeptidase-C digestion of the CuOOH-inactiv

21 grates with a peptide that is released after CNBr cleavage of bacterially produced-recombinant hINV.

22 ) that yielded, upon photoligand binding and CNBr digestion, a broad protein band of approximately 46

23 the acidic conditions of HPLC separation and CNBr digestion.

24 generate DNA primers based on N-terminal and CNBr cleavage fragment amino acid sequences of T. pallid

25 Electrophoresis of a cyanogen bromide (CNBr) (CB) digest of sternal cartilage revealed an alpha

26 have previously shown that cyanogen bromide (CNBr) cleavage of cornified envelopes isolated from cult

27 ntified by MALDI-MS of its cyanogen bromide (CNBr) cleavage products.

28 rmic acid and subjected to cyanogen bromide (CNBr) cleavage, and the pattern of chemically generated

29 analysis of the C-terminal cyanogen bromide (CNBr) fragment, and comparison of recognition by epitope

30 Cyanogen bromide (CNBr) is a common chemical used to hydrolyze peptide bon

31 followed by digestion with cyanogen bromide (CNBr) or trypsin.

32 und to GAMP activated with cyanogen bromide (CNBr) or with 1-cyano-4(dimethylamino)-pyridinium tetraf

33 arides were activated with cyanogen bromide (CNBr) or with 1-cyano-4-dimethylaminopyridinium tetratfl

34 eptor using Endo Lys C and cyanogen bromide (CNBr) revealed that the [ (125)I]-N-IACoc label was loca

35 nd further localized using cyanogen bromide (CNBr), which hydrolyzes proteins on the C-terminal side

36 ine as the spacer arm to a cyanogen bromide (CNBr)-activated-Sepharose 4B matrix.

37 ipidated, and cleaved with cyanogen bromide (CNBr).

38 a-tubulin was cleaved with cyanogen bromide (CNBr).

39 ation and was cleaved with cyanogen bromide (CNBr).

40 modification was determined to be Tyr-236 by CNBr peptide mapping and automated peptide sequencing.

41 autophosphorylated in vitro and analyzed by CNBr cleavage.

42 due peptide was released from its carrier by CNBr and obtained in wild-type, (15)N, and (13)C/(15)N f

43 modified subunits were chemically cleaved by CNBr and then purified by HPLC using a C18 column.

44 tion were reduced, alkylated, and cleaved by CNBr.

45 present in active rSMB were investigated by CNBr cleavage, partial reduction and S-alkylation, mass

46 -linking on the beta1 chain was localized by CNBr peptide mapping within residues 130-146, a region t

47 was determined to be within Ala206-Met243 by CNBr cleavage of partially purified labeled mu receptors

48 ed SMB in aqueous solution, and prepared, by CNBr cleavage, the N-terminal segment of 51 amino acid r

49 Five alpha chain CNBr fragments (within Aalpha 208-610) and one gamma cha

50 (within Aalpha 208-610) and one gamma chain CNBr fragment (gamma 385-411) were the only portions of

51 Enzymatic (Glu-C and Lys-C) and chemical (CNBr and BNPS-skatole) digestions of the photoconjugate

52 otein characterization approaches [chemical (CNBr) and proteolytic (lysylendopeptidase-C) digestion,

53 In spite of these structural differences, CNBr cleavage releases an identical quartet of hINV-immu

54 s-linked to Val-Arg-Lys-Ala-Hse (an expected CNBr fragment of FPR, residues 83-87).

55 In parallel experiments, CNBr-fragmented XFM was separately digested in solution

56 Direct analysis of the growth factor CNBr digest showed 7542.99, 4993.4, and 3107.7 Da peptid

57 epresents the predicted cleavage product for CNBr/trypsin and corresponds to amino acids Arg(174)-Met

58 ed proteins and of peptides that result from CNBr digestion of proteins on the nitrocellulose membran

59 BSA was bound to activated GAMP to form GAMP(CNBr)-AHBSA and GAMP(CDAP)-AHBSA.

60 dinium tetrafluoroborate (CDAP) to form GAMP(CNBr)AH and GAMP(CDAP)AH.

61 aminopropyl) carbodiimide (EDC) to form GAMP(CNBr)AH-BSA and GAMP(CDAP)AH-BSA.

62 high-resolution isoelectric focusing, in-gel CNBr cleavage, and mass spectrometry were combined, we d

63 I activity and the protein was identified in CNBr extracts of purified keratinocytes cornified envelo

64 in combinations that would generate labeled CNBr fragments of distinct masses depending on the label

65 lar weight and sequence data from bovine MIP CNBr fragments, directly or after subsequent digestion w

66 Analysis of CNBr digestion fragments confirms that two disulfide bri

67 rate determination, coupled with analysis of CNBr digestion fragments, confirms N-linked glycosylatio

68 Analysis of CNBr-digested cPLA(2)gamma by matrix-assisted laser deso

69 In the case of CNBr digests, for example, modified methionine residues

70 by limited hydrolysis with a combination of CNBr and chymotrypsin under nonreducing, nonalkylating c

71 alogues have been mapped by a combination of CNBr digestion and immunoprecipitation studies.

72 munoprecipitation and secondary digestion of CNBr fragments with endoproteinase Lys-C.

73 man MIP sequence was observed in the form of CNBr fragments.

74 of the molecule and a C-terminal fragment of CNBr-cleaved recombinant EbpS, however, did not interact

75 s mapped by molecular weight measurements of CNBr fragments, confirming the reported DNA sequence.

76 s spectroscopy and direct microsequencing of CNBr fragments of phospho-moesin, the phosphorylation si

77 d from the cDNA agrees with the sequences of CNBr fragments of eIF-3, confirming the identity of the

78 Electrospray ionization mass spectrometry of CNBr fragments of the 35-kDa polypeptide was diagnostic

79 result confirmed by selective suppression of CNBr-mediated cleavage of beta-III tubulin.

80 Protein sequence data on CNBr fragments of purified FP21 showed that both gene pr

81 ab was proteolyzed, using proteinase ArgC or CNBr, and the peptides derived were analyzed by tandem m

82 hodologies were employed to isolate purified CNBr fibrin fragments whose structures included the acce

83 fide-linked peptides generated by sequential CNBr and pepsin treatment of radiolabeled PHMcc were sep

84 The NH2 terminus was blocked, so CNBr digestion was used to generate internal peptides.

85 atidylcholine, the N-terminal and C-terminal CNBr fragments of apoA-I each bound to SR-BI in a satura

86 e of complexing with FBG and with N-terminal CNBr fragments of FBG (NDSK) and of fibrin (IIa-NDSK), b

87 The CNBr and trypsin peptides were analyzed by liquid chroma

88 The CNBr digest was resolved according to peptide size by ge

89 The CNBr fragment generated from the 3'-BzDC-Taxol-photolabe

90 the similarity in molecular mass between the CNBr digest of the (125)I-K27-[L261M]hPTH1-Rc conjugate

91 In contrast, the CNBr fragment generated from the 7-BzDC-Taxol-photolabel

92 eptide also competes with a component of the CNBr digestion fraction of lactoferrin for Ab binding in

93 These residues overlap most of the CNBr fragment containing the second cluster of complemen

94 Further cleavage of the CNBr peptides by trypsin and Lys-C protease, followed by

95 Identification of the CNBr-cleaved fragments of CRFR1 cross-linked to (125)I-Y

96 oth of the membrane-bound protein and of the CNBr-cleaved peptides, allows the site of cleavage to be

97 pecies with mass = 1754, consistent with the CNBr fragment of fMBpaFYK-fl cross-linked to Val-Arg-Lys

98 ity in human cell lines by analysis of their CNBr-released C-terminal peptides.

99 the methionyl-serine and methionyl-threonine CNBr cleavage inefficiencies and have developed a simple

100 zide ligand and the l-tyrosine spacer-arm to CNBr-activated-Sepharose-4B.

101 matography with purified annexins coupled to CNBr-activated Sepharose 4B was used to determine the ca

102 Purified fimbriae were coupled to CNBr-activated Sepharose-4B, and the solubilized epithel

103 Furthermore, resistance to CNBr cleavage and dual NMR resonances of porcine and hum

104 linked product was isolated and subjected to CNBr cleavage.

105 0-90,000, which were pooled and subjected to CNBr digestion for primary amino acid sequence analysis.

106 masses of the human alpha- and beta-tubulin CNBr-derived C-terminal peptides are all in the 1500--40

107 Sequences obtained from two CNBr-derived fragments of this protein matched lipoprote

108 the same internal amino acid sequences upon CNBr digestion, and have molecular mass values agreeing

109 se hamster ovary membranes were cleaved with CNBr, and the fluorescent fragments were isolated on an

110 Fusion proteins were digested with CNBr and re-Hsts were purified by reversed-phase high pe

111 mately 50 kDa) was excised and digested with CNBr to release the highly divergent C-terminal tubulin

112 Sequential digestion of this protein with CNBr/trypsin revealed photolabeling of a 2.9-kDa peptide