Correction to the Amino Acid Sequence of Porcine Motilin

1974 ◽  
Vol 52 (1) ◽  
pp. 7-8 ◽  
Author(s):  
Harold Schubert ◽  
John C. Brown
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Leucine Aminopeptidase ◽  
Kinetic Studies ◽  
Natural Material ◽  
Synthetic Analogue ◽  
Tryptic Peptides ◽  
Electrophoretic Mobilities ◽  
Acidic Peptide

A comparison of the electrophoretic mobilities of the tryptic peptides of natural porcine motilin and a synthetic analogue with norleucine substituted for methionine revealed the absence of the acidic peptide TR3 of the natural material. Kinetic studies with leucine aminopeptidase and dansyl-Edman degradations on this peptide revealed the presence of glutamine at position 14 and not glutamic acid as previously reported. It is suggested that in the earlier preparation of natural porcine motilin deamidation of glutamine occurred.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1963 ◽  
Vol 18 (12) ◽  
pp. 1032-1049 ◽  
Author(s):  
B. Wittmann-Liebold ◽  
H. G. Wittmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Acid Sequences ◽  
Tryptic Peptides

The amino acid sequence of dahlemense, a naturally occuring strain of tobacco mosaic virus, has been determined and compared with that of the strain vulgare (Fig. 7). In this communication the experimental details are given for the elucidation of the amino acid sequences within two tryptic peptides with 65 amino acids.

scholarly journals The amino acid sequence of a glutamic acid-rich protein from bovine retina as deduced from the cDNA sequence.

1991 ◽  
Vol 88 (8) ◽  
pp. 3116-3119 ◽  
Author(s):  
Y. Sugimoto ◽  
K. Yatsunami ◽  
M. Tsujimoto ◽  
H. G. Khorana ◽  
A. Ichikawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Cdna Sequence ◽  
Bovine Retina

scholarly journals Primary Structure of Human Platelet Factor 4.

1977 ◽  
Author(s):  
F.J. Morgan ◽  
G.S. Begg ◽  
C.N. Chesterman
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Information ◽  
Human Platelet ◽  
Specific Protein ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Tryptic Peptides

The amino acid sequence of human platelet factor 4 (PF4) has been studied. PF4 is a platelet specific protein with antiheparin activity, released from platelets as a proteoglycan complex, whose measurement may provide an important index of platelet activation both in vivo and in vitro. These studies were undertaken to characterize fully the PF4 molecule. PF4 is a stable tetramer, composed of identical subunits, each with a molecular weight based on the sequence studies of approx. 7,770. Each PF4 subunit contains 69 amino acids, including 4 half-cystine (# 10, 12, 36, 37), one tyrosine (# 59), 3 arginine and 8 lysine, but no methionine, phenylalanine or tryptophan residues. The basic residues are predominantly in the C-terminal region. The tryptic peptides were aligned after studies which included tryptic digestion of citraconylated RCM-PF4, and automated Edman degradation of RCM-PF4 and citraconylated tryptic peptides. No glycopeptides were detected. This structural information should enable clear distinction to be made between PF4 and other platelet proteins such as β thromboglobulin. The provisional amino acid sequence of each subunit is:Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser-Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Cys-Pro-Thr-Ala-Gln-Ile-Leu-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Pro-Leu-Asp-Leu-Gln-Ala-Tyr-Leu-Lys-Ile-Lys(Lys, Lys, Ser, Glx, Leu, Leu)

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