Analysis amino acid sequence

Firefly. Firefly luciferase (EC 1.13.12.7) is a homodimeric enzyme (62 kDa subunit) that has binding sites for firefly luciferin and Mg ATP . Amino acid sequence analysis has iadicated that beetle luciferases evolved from coen2yme A synthetase (206). Firefly bioluminescence is the most efficient bioluminescent reaction known, with Qc reported to be 88% (5), and at 562 nm (56). At low pH and ia the presence of certain metal ions (eg, Pb ", ... 

Amino acid sequence analysis reveals that proteins with related functions often show a high degree of sequence similarity. Such findings suggest a common ancestry for these proteins. 

The calculated value for the Hisg-tagged protein is 28,492 Da. N-terminal amino acid sequence analysis (Procise) was carried out on purified recombinant resilin. The following sequence (at 120 pmol yield) was obtained for the first 12 amino acid residues MHHHHHHPEPPV, as expected from DNA sequence analysis. 

The Edman reaction enabled amino acid sequence analysis to be automated. Mass spectrometry provides a sensitive and versatile tool for determining primary strucmre and for the identification of post-translational modifications. 

In the last few years additional members of the interferon family has been discovered. Amino acid sequence analysis of a protein called trophoblastin (which is found in many ruminants) revealed... 

Although this chapter did not discuss much about the amino acid sequence analysis per se, such as sequence comparison, motif detection, and structure prediction, the sequence analysis is a prerequisite of the network analysis. In fact, the network analysis is an integrated analysis of sequence and other information. For example, in the graph comparison of two pathways, it is not only the overall arrangements of nodes... 

Leppard K, Totty N, Waterfield M, Harlow E, Jenkins J, Crawford L. 1983. Purification and partial amino acid sequence analysis of the cellular tumour antigen, p53, from mouse SV40-transformed cells. Embo J 2 1993-1999. 

In the last few years additional members of the IFN family has been discovered. Amino acid sequence analysis of a protein called trophoblastin—which is found in many ruminants — revealed that it was closely related to IFN-a. This result was surprising because, in sheep and several other ruminants, the primary function (and until recently the only known function) of trophoblastin is to sustain the corpus luteum during the early stages of pregnancy. The 172 amino acid protein is produced by the trophoblast (an outer layer of cells which surround the cells that constitute the early embryo) for several days immediately preceding implantation. In many ruminants, therefore, trophoblastin plays an essentially similar role to hCG in humans (Chapter 8). 

Partial amino acid sequence analysis. The sequence data permit confirmation of the correct N-terminal processing and detection of the loss of the C-terminal amino acids. 

Proteins blotted on PVDF membranes are stainable with Coomassie Brilliant Blue R250, but a relative intense background remains, which does not influence, for example, amino acid sequence analysis. 

He, X.Z. and Dixon, R.A., Affinity chromatography, substrate/product specificity, and amino acid sequence analysis of an isofiavone 0-methyltransferase from alfalfa (Medicago sativa L.). Arch. Biochem. Biophys., 336, 121, 1996. 

Hunkapiller, M. W, Lujan, E., Ostrander, F., and Hood, L. E. (1983) Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 91, 227-236. 

VII. Amino Acid Sequence Analysis of the Small Proteoglycan Core Protein, Deduced... 

About 40% of human immunoglobulin light chains are X (Hood et al., 1967). Early studies of X chains produced by patients with multiple myeloma identified four types of C regions that were distinguished serologically and/or by amino acid sequence analysis they appeared not to be allelic and were presumed to be the products of distinct C genes (Appella and Ein, 1967 Ein and Fahey, 1967 Ein, 1968 Hess et al., 1971 Gibson et al., 1971 Fett and Deutsch, 1975). 

Eckerskom, C. and Lottspeich, F. (1993) Structural characterization of blotting membranes and the influence of membrane parameters for electroblotting and subsequent amino acid sequence analysis of proteins. Electrophoresis 14, 831-838. 

The purification of HCV14 2A protein after each column is summarized in Fig. 2. As seen in Fig. 2, the protein had a molecular weight of —16 kDa, matching its estimated molecular mass of 15,976 Da. The identity of this purified protein as HRV14 2A was further confirmed by mass spectrometric analysis (data not shown). Amino acid sequence analysis was also performed on the purified HRV14 2A protein. Its N-terminal amino acids were identified as GLGPRYGGIYTSN-, which was identical to the expected sequence. 

Amino acid sequence analysis of the human 5-HT1B receptor has revealed consensus phosphorylation sites in all intracellular loops for PKA and PKC. Phosphorylation of the 5-HT1B receptor was demonstrated by metabolic labeling of the 5-HTib receptor-expressing Sf9 cells with [32Pi]phosphate (141). This posttranslational modification was proposed to be involved in receptor regulation such as desensitization. 

Furthermore, it was shown that there are three different isoforms of tropomyosin relating to different functional needs (fast, slow-twitch, and slow-tonic), identified by amino acid sequence analysis (Motoyama et al. 2007). The fast isoform is mostly found in the abdominal muscle (tail), while the slow isoform is mainly associated with muscle obtained from the legs however, both forms can be found in abdominal and leg muscle, with an amino acid homology of up to 100%. 

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