Amino-terminal Amino-acid Sequences of Human Plasma 3S γ1-Globulin and Carbonic Anhydrase B

Nature ◽  
1967 ◽  
Vol 215 (5096) ◽  
pp. 66-67 ◽  
Author(s):  
T. IKENAKA ◽  
K. SCHMID
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Human Plasma ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Carbonic Anhydrase B ◽  
Terminal Amino

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Biochemistry ◽  
1978 ◽  
Vol 17 (3) ◽  
pp. 442-445 ◽  
Author(s):  
Mark A. Hermodson ◽  
Kirk C. S. Chen ◽  
Thomas M. Buchanan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Unusual Amino Acid

scholarly journals Rice Embryo Globulins: Amino-Terminal Amino Acid Sequences, cDNA Cloning and Expression

1996 ◽  
Vol 37 (5) ◽  
pp. 612-620 ◽  
Author(s):  
J.-L. Sun ◽  
H. Nakagawa ◽  
S. Karita ◽  
K. Ohmiya ◽  
T. Hattori
Keyword(s):  
Amino Acid ◽  
Cdna Cloning ◽  
Amino Acid Sequences ◽  
Cloning And Expression ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Rice Embryo

scholarly journals Alpha and beta chains of SB and DR antigens are structurally distinct

1982 ◽  
Vol 156 (5) ◽  
pp. 1557-1562 ◽  
Author(s):  
CK Hurley ◽  
S Shaw ◽  
L Nadler ◽  
S Schlossman ◽  
JD Capra
Keyword(s):  
Amino Acid ◽  
Cell Line ◽  
Amino Acid Sequences ◽  
Beta Chain ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino

Limited amino-terminal amino acid sequences of the HLA-controlled SB and DR antigens from the cell line PREISS (DR4/4, SB3/4) show differences in both the alpha and beta chain sequences of the two molecules. SB antigens, like DR antigens, appear to be homologues of the murine I-E antigens.

scholarly journals Amino-terminal amino acid sequences and the evolution of frog (Rana esculenta ) trypsin and chymotrypsin

FEBS Letters ◽  
1980 ◽  
Vol 109 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Wolfgang Pies ◽  
Robert Zwilling ◽  
Richard G. Woodbury ◽  
Hans Neurath
Keyword(s):  
Amino Acid ◽  
Rana Esculenta ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino

A major Litomosoides carinii microfilarial sheath glycoprotein (gp22): amino terminal sequence and immunological studies with corresponding synthetic peptides

Parasitology ◽  
1991 ◽  
Vol 103 (3) ◽  
pp. 387-394 ◽  
Author(s):  
G. Bardehle ◽  
F. J. Conraths ◽  
F. Fahrenholz ◽  
M. Hintz ◽  
D. Linder ◽  
...  
Keyword(s):  
Amino Acid ◽  
Synthetic Peptides ◽  
General Pattern ◽  
Amino Sugar ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Amino Terminal Sequence

The major glycoprotein of the sheath of Litomosoides carinii microfilariae (gp22) was analysed for its amino acid and amino sugar composition. It is rich in proline, glutamine/glutamic acid and glycine and contains (N-acetyl)galactosamine. The N-terminal amino acid sequence was determined up to position 37. It consists of a group of 6 repeats of the pentapeptide sequence methionine-glycine-proline-glutamine-proline with two minor modifications in repeats 3–6, while the first two repeats follow the general pattern more loosely. Identical N-terminal amino acid sequences were found in at least two other sheath polypeptides (33 kDa, 39 kDa). Antisera prepared against 3 overlapping synthetic peptides corresponding to the amino terminus of gp22 recognized different epitopes. They all reacted with identical patterns of sheath polypeptides. The antisera failed to recognize antigens of 4th-stage larvae of L. carinii. In contrast, cross-reacting epitopes were detected in other parasite stages. Antisera reacted with material surrounding embryos and microfilariae in the uterus of females, and caused patchy fluorescence on the sheath of blood-derived and in vitro-released microfilariae.

THE USE OF REGION SPECIFIC RADIOIMMUNOASSAYS FOR CHARACTERIZATION OF CIRCULATING CALCITONIN IN PATIENTS WITH MEDULLARY CARCINOMA OF THE THYROID GLAND

1979 ◽  
Vol 91 (3) ◽  
pp. 449-461 ◽  
Author(s):  
Lisbeth Myhre ◽  
Kaare M. Gautvik
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Molecular Forms ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Terminal Amino ◽  
Carboxy Terminal ◽  
Amino Terminal Fragment

ABSTRACT Two antisera with known region specificities have been used to characterize calcitonin immunoreactivity (iCT) in serum of patients with medullary thyroid carcinoma (MCT). Antiserum I which was raised against the synthetic hormone (1–32 amino acid residues), contained heterogeneous populations of immunoglobulins directed predominantly against carboxyterminal sequences of the hormone, but the antiserum reacted also with the amino-terminal fragment (1–10 amino acid residues). Antiserum II, which was raised against the carboxy-terminal hormone fragment (11–32 amino acid residues) reached equally well with the intact hormone and the C-terminal fragment, but showed negligible binding of the amino terminal fragment. Antiserum I measured therefore both amino-terminal and carboxy-terminal sequences of calcitonin while antiserum II measured only carboxy-terminal amino acid sequences. In 40 patients with MCT, antiserum I measured usually the highest concentration of serum iCT suggesting the presence of non-uniform hormone immunoreactivity. The different molecular forms of circulating iCT in 7 MCT patients were explored by using antiserum I after gel filtration on Sephadex G-100. The patients who were selected on basis of iCT measurement in serum using antiserum I and II, could be divided into 3 groups which showed characteristic iCT profiles. Group 1, in which antiserum II measured a higher concentration of serum iCT, contained predominantly (60–70 %) small fragments of calcitonin immunoreactivity. On the other hand, in the sera of group 3 in which antisera I measured an equal or the highest concentrations, the dominant form of the hormone consisted of molecular sequences equal to or larger than the intact hormone (90 %). In group 2, the two antisera measured an equal amount of serum iCT and molecular forms consisting mostly of larger hormone fragments dominated (50 %). All the patients were normocalcaemic in spite of frequently grossly elevated serum iCT, and 33 out of 36 patients had normal serum immunoreactive parathyroid hormone. In conclusion: 1. Serum iCT is heterogeneous and represents peptides of quite different molecular size with no or low biological activity. 2. Most of the serum calcitonin immunoreactivity consists of peptides with carboxy-terminal amino acid sequences. 3. Most, if not all, of the amino-terminal calcitonin immunoreactivity is due to monomeric and polymeric hormonal forms.

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