Results 161 to 170 of about 503,832 (211)

Amino acid sequence homology among fructose-1,6-bisphosphatases

Biochemical and Biophysical Research Communications, 1986
The hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate is a key reaction of carbohydrate metabolism. The enzyme that catalyzes this reaction, fructose-1,6-bisphosphatase, appears to be present in all forms of living organisms. Regulation of the enzyme activity, however, occurs by a variety of distinct mechanisms.
F, Marcus, B, Gontero, P B, Harrsch, J, Rittenhouse   +3 more
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Amino acid sequence homologies in alfa-sarcin, restrictocin and mitogillin

Biochemical and Biophysical Research Communications, 1982
Abstract The NH2-terminal amino acid sequence of the three anti-tumor proteins, alfa-sarcin, mitogillin and restrictocine, has been determined for 20 cycles by automated sequencing procedure. A high degree of sequence homology was observed in this region of the molecule.
R, Rodriguez, C, Lopez-Otin, D, Barber, J L, Fernandez-Luna, G, Gonzalez, E, Mendez   +5 more
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Synaptic Cleft Glycoproteins Contain Homologous Amino Acid Sequences

Science, 1982
The concanavalin A--binding glycoproteins of the rat synaptic junction were isolated by affinity chromatography. These glycoproteins had molecular weights of 160,000, 123,000, 110,000, and 95,000. The tryptic peptide maps of these glycoproteins showed that the three largest glycoproteins contained a high percentage of identical peptides. This indicates
E E, Mena, C W, Cotman
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Amino Acid Sequence of a Purothionin Homolog from Barley Flour

The Journal of Biochemistry, 1980
A purothionin homolog was isolated from barley flour and purified by CM-52 column chromatography. It showed potent lethal activity towards brewer's yeast and its complete amino acid sequence was determined to be as follows. Lys-Ser-Cys-Cys-Arg-Ser-Thr-Leu-Gly-Arg-Asn-Cys-Tyr-Asn-Leu-Cys-Arg-Val-Arg-Gly-Ala-Gln-Lys-Leu-Cys-Ala-Gly-Val-Cys-Arg-Cys-Lys ...
Y, Ozaki, K, Wada, T, Hase, H, Matsubara, T, Nakanishi, H, Yoshizumi   +5 more
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Amino-Terminal Amino Acid Sequence of the Silkworm Prothoracicotropic Hormone: Homology with Insulin

Science, 1984
Three molecular forms of prothoracicotropic hormone were isolated from the head of the adult silkworm, Bombyx mori , and the amino acid sequence of 19 amino acid residues in the amino terminus of these prothoracicotropic hormones was determined.
H, Nagasawa, H, Kataoka, A, Isogai, S, Tamura, A, Suzuki, H, Ishizaki, A, Mizoguchi, Y, Fujiwara, A, Suzuki   +8 more
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Correspondence of homologies in amino acid sequence and tertiary structure of protein molecules

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
According to the method developed previously (Kubota, Y., Takahashi, S., Nishikawa, K. and Ooi, T. (1981) J. Theor, Biol. 91, 347-361), homology among proteins may be estimated quantitatively. We extended the method to investigate the relationship of an amino acid sequence to its teritary structure and identify homologous segments which have homologous
Y, Kubota, K, Nishikawa, S, Takahashi, T, Ooi   +3 more
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Amino acid sequence homology between bovine and human platelet proteins

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985
The complete amino acid sequence of bovine platelet factor 4 (PF-4) was determined. Comparison of the 88 residue bovine protein with its 70 residue human counterpart indicated 73% homology. There is 53% homology between this bovine protein and another human platelet protein, beta-thromboglobulin (beta-TG).
R E, Ciaglowski, D A, Walz
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Complete amino acid sequence of streptokinase and its homology with serine proteases

Biochemistry, 1982
The complete amino acid sequence of streptokinase has been determined by automated Edman degradation of its cyanogen bromide and proteolytic fragments. The protein consists of 415 amino acid residues. Sequence microheterogeneity was found at two positions.
K W, Jackson, J, Tang
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Structural domains of phytochrome deduced from homologies in amino acid sequences

Journal of Protein Chemistry, 1992
A method of semiempirical identification of structural domains is proposed. The procedure is based on the comparison of amino acid sequences in groups of homologous proteins. This approach was tested using 32 known protein sequences from different cytochrome b5, cytochrome c, lysozyme, hemoglobin, and myoglobin proteins.
M, Romanowski, P S, Song
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Transformational Homologies in Amino Acid Sequences Suggest Memberships in Protein Families

Journal of Statistical Physics, 1998
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Mandell, Arnold J., Selz, Karen A., Shlesinger, Michael F.   +2 more
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