scholarly journals The amino acid sequence around the reactive serine residue in alkaline phosphatase of Serratia marcescens

1964 ◽  
Vol 92 (2) ◽  
pp. 421-422 ◽  
Author(s):  
N Zwaig ◽  
C Milstein
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serratia Marcescens ◽  
Serine Residue

scholarly journals Factor D̄ of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site

1980 ◽  
Vol 187 (3) ◽  
pp. 863-874 ◽  
Author(s):  
D M Johnson ◽  
J Gagnon ◽  
K B Reid
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Alternative Pathway ◽  
Amino Acid Sequences ◽  
Serine Residue ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The serine esterase factor D of the complement system was purified from outdated human plasma with a yield of 20% of the initial haemolytic activity found in serum. This represented an approx. 60 000-fold purification. The final product was homogeneous as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (with an apparent mol.wt. of 24 000), its migration as a single component in a variety of fractionation procedures based on size and charge, and its N-terminal amino-acid-sequence analysis. The N-terminal amino acid sequence of the first 36 residues of the intact molecule was found to be homologous with the N-terminal amino acid sequences of the catalytic chains of other serine esterases. Factor D showed an especially strong homology (greater than 60% identity) with rat ‘group-specific protease’ [Woodbury, Katunuma, Kobayashi, Titani, & Neurath (1978) Biochemistry 17, 811-819] over the first 16 amino acid residues. This similarity is of interest since it is considered that both enzymes may be synthesized in their active, rather than zymogen, forms. The three major CNBr fragments of factor D, which had apparent mol.wts. of 15 800, 6600 and 1700, were purified and then aligned by N-terminal amino acid sequence analysis and amino acid analysis. By using factor D labelled with di-[1,3-14C]isopropylphosphofluoridate it was shown that the CNBr fragment of apparent mol.wt. 6600, which is located in the C-terminal region of factor D, contained the active serine residue. The amino acid sequence around this residue was determined.

scholarly journals The amino acid sequence around the reactive serine residue of some proteolytic enzymes

1960 ◽  
Vol 77 (1) ◽  
pp. 149-163 ◽  
Author(s):  
M. A. Naughton ◽  
F. Sanger ◽  
B. S. Hartley ◽  
D. C. Shaw
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzymes ◽  
Serine Residue

Amino acid sequence in the region of the reactive serine residue of eel acetylcholinesterase

Biochemistry ◽  
1973 ◽  
Vol 12 (15) ◽  
pp. 2946-2950 ◽  
Author(s):  
Norwood K. Schaffer ◽  
Harry O. Michel ◽  
Alec F. Bridges
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Residue

Amino Acid Sequence Studies of Horseradish Peroxidase. II. Thermolytic Peptides

1972 ◽  
Vol 50 (1) ◽  
pp. 63-90 ◽  
Author(s):  
K. G. Welinder ◽  
L. B. Smillie
Keyword(s):  
Amino Acid ◽  
Horseradish Peroxidase ◽  
Amino Acid Sequence ◽  
Cation Exchanger ◽  
Paper Electrophoresis ◽  
Tryptophan Residue ◽  
Amino Acid Residues ◽  
Disulfide Bridges ◽  
Serine Residue ◽  
C Terminus

Horseradish peroxidase (HRP) was digested with thermolysin. On fractionation on Sephadex G-25, Fine Chromobeads type P (Dowex 50 type resin) and by high-voltage paper electrophoresis, we isolated about 120 thermolytic peptides. Some experimentation on the composition of the pyridine acetate gradient, used for elution of the cation exchanger, is reported. All peptides were characterized with respect to amino acid composition, N-terminal residue, and pH 6.5 mobility. Unknown peptides or peptides not corresponding unambiguously to previously established tryptic sequences were subjected to dansyl-Edman analysis. Thermolytic peptides accounting for all tryptic sequences except a dipeptide and a tripeptide, and unique thermolytic sequences accounting for about 100 amino acid residues, were obtained. Nine convincing and several indicative overlaps were established for known tryptic sequences. The sequences around all four disulfide bridges, the three histidine residues, and the only tryptophan residue have been elucidated. Eight sites of carbohydrate attachment have been identified. For seven of these sites we have evidence for attachment to asparagine, and for six of the sites the carbohydrate-bound asparagine was found in the well-known sequences Asn–X–Ser/Thr. The remaining two sequences, though incomplete, are compatible with this pattern. Tentatively we suggest a pyrrolidone carboxyl N-terminal for HRP. The specificity of trypsin implicates a sequence found in two varieties, differing only by a C-terminal serine residue at the C-terminus of HRP. A discussion of the possible complications of the acidic heme extraction on the results obtained is included.

Sign in / Sign up

Export Citation Format

Share Document