Amino Acid Composition and Influence of the Modification of Some Amino Acid Residues on the Catalytic Activity of the Spleen Exonuclease

1988 ◽  
pp. 233-236
Author(s):  
A. T. Bakalova ◽  
L. B. Dolapchiev
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Residues

scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase

1973 ◽  
Vol 133 (4) ◽  
pp. 805-819 ◽  
Author(s):  
Francesco Bossa ◽  
Donatella Barra ◽  
Massimo Carloni ◽  
Paolo Fasella ◽  
Francesca Riva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Science And Technology ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Lending Library

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

scholarly journals The cDNA and protein sequences of human lactate dehydrogenase B

1987 ◽  
Vol 248 (3) ◽  
pp. 933-936 ◽  
Author(s):  
I Sakai ◽  
F S Sharief ◽  
Y C Pan ◽  
S S Li
Keyword(s):  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Sequences ◽  
British Library ◽  
Amino Acid Residues ◽  
Coding Region ◽  
Cdna Insert ◽  
Protein Coding

Human lactate dehydrogenase B (LDH-B) cDNA was isolated and sequenced. The LDH-B cDNA insert consists of the protein-coding sequence (999 bp), the 5′ (54 bp) and 3′ (203 bp) non-coding regions, and the poly(A) tail (50 bp). The predicted sequence of 333 amino acid residues was confirmed by amino acid composition and/or sequence analyses of a total of 185 (56%) residues from tryptic peptides of human LDH-B protein. The nucleotide and amino acid sequences of the human LDH-B coding region show 68% and 75% homologies respectively with those of the human LDH-A. The peptide map and amino acid composition data have been deposited as Supplementary Publication SUP 50139 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

scholarly journals Studies of haemoglobin types in barbary sheep (Ammotragus lervia)

1968 ◽  
Vol 107 (6) ◽  
pp. 745-751 ◽  
Author(s):  
G. van Vliet ◽  
T. H. J. Huisman ◽  
G. A. Dasher ◽  
W. H. Moretz ◽  
A. M. Dozy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Domestic Sheep ◽  
Amino Acid Residues ◽  
Amino Acid Compositions ◽  
Ammotragus Lervia ◽  
Peptide T ◽  
Barbary Sheep ◽  
Β Chain

1. Two haemoglobin types, haemoglobins Amm-C and Amm-B, were observed in five Barbary sheep (Ammotragus lervia). One animal was homozygous for haemoglobin Amm-C, a second was homozygous for haemoglobin Amm-B, and three were heterozygous for both. 2. Amino acid analyses of the globin from haemoglobin Amm-B showed that this type was related to, but not identical with, haemoglobin B of the domestic sheep. 3. The β-chain of haemoglobin Amm-C was found to be composed of 141 amino acid residues. Its amino acid composition differed from that of the βC-chain of the anaemic domestic sheep in at least 14 residues. The Amm-βC-chain contained one isoleucyl residue. 4. The amino acid compositions of tryptic peptides T-1, T-2, T-13 and T-14 of the Amm-βC-chain were similar to those of the sheep βC-chain. Peptides T-3, T-4, T-6, T-7, T-8, T-11 and T-15 were the same as the corresponding peptides of the sheep βA- and βC-chains. Peptide T-5 and to a smaller extent peptide T-9 resembled the corresponding peptides of the sheep βA-chain, and peptide T-10 was identical with peptide γT-10 of sheep haemoglobin F. Peptide T-12 was not recovered. 5. The results of these investigations were interpreted as being indicative that the structural Amm-βC-gene is closely related to the βC-gene of sheep, from which through domestication the present domestic sheep originated.

scholarly journals Purification and crystallization of avidin

1970 ◽  
Vol 118 (1) ◽  
pp. 67-70 ◽  
Author(s):  
N. M. Green ◽  
E. J. Toms
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Egg White ◽  
Amino Acid Residues ◽  
Equivalent Weight ◽  
Integral Number ◽  
Hen’S Egg

An improved purification, including crystallization, of avidin from hen's-egg white is described. The product bound 15.1μg of biotin/mg, corresponding to an equivalent weight of 16200. The amino acid composition showed an integral number of amino acid residues per 16200g, which suggested that each molecule of avidin (mol. wt. approx. 66000) contained four identical subunits.

Amino Acid Composition of Myosin from Trout Muscle

1967 ◽  
Vol 24 (7) ◽  
pp. 1607-1612 ◽  
Author(s):  
H. Buttkus
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
White Muscle ◽  
Apparent Molecular Weight ◽  
Amino Acid Residues ◽  
Density Measurements ◽  
Composition Formula ◽  
Thermal Stability Of ◽  
Trout Muscle

The amino acid composition of myosin from the white muscle of trout has been determined and was found to be closely similar to that of rabbit myosin. Thirteen of the amino acid residues were present in concentrations identical to those of rabbit myosin or agreed within less than 3%. Valine, glycine, and methionine were present in slightly greater proportions. The histidine and proline contents of trout myosin differed from rabbit myosin by three residues per 105 g of protein and represented the greatest difference on a per cent basis. The possible significance of these differences is discussed in relation to the lower enzymatic activity and the lower thermal stability of trout myosin. The apparent specific volume of trout myosin calculated from the amino acid composition [Formula: see text] was identical to that obtained by density measurements. An apparent molecular weight calculated from the amino acid analyses was 500,027 ± 44.

ORNITHO-KININOGEN: ITS ISOLATION AND CHARACTERIZATION

1987 ◽  
Author(s):  
M Kimura ◽  
T Sueyoshi ◽  
T Morita ◽  
K Tanaka ◽  
S Iwanaga
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Reversed Phase ◽  
Amino Acid Residues ◽  
Isolation And Characterization ◽  
Bovine Plasma ◽  
Sds Page ◽  
Plasma Kinins

In mammals, three kinds of kininogens, high-Mr kininogen, low-Mr kininogen and T-kininogen, are known and their structures and functions have been well studied. However, little is known about non-mammalian kininogens and their existence has been known only by the release of plasma kinins. In 1966, Werle et al. reported that an ornitho-kinin liberated by tissue kallikrein from chicken, plasma differs;from mammalian kinins in its amino acid composition. Since that, there is no report about the structure of ornitho-kinin.In this study, ornitho-kininogen was isolated from chicken plasma by two steps with S-alkylated papain affinity and DEAE-5PW columns. The yield was 1.7 mg from 44 ml of plasma. The purified material gave a single band on SDS-PAGE with or without 2-mercaptoethanoL and on disc-PAGE, and the molecular weight was estimated to be 74,000 on SDS-PAGE by Ferguson plot. Ornitho-kininogen seemed to belong to mammalian high-Mr kininogen, based on the amino acid composition, and the molecular weight, and no kininogen corresponding to low-Mr kininogen and T kininogen was found in chicken plasma. In fact, ornitho-kininogen was degraded rapidly by bovine plasma kallikrein, liberating an ornitho-kinin, and the resulting kinin was separated by reversed phase HPLC on a column of Cosmosil 5C18-P. The amino acid sequence of ornitho-kinin was established to be Arg-Pro-Pro-Gly-Phe-Thr-Pro-Leu-Arg, in which the composition was different from that reported earlier by Werle et al. This sequence was similar to that of bradykinin but the two substitutions of Thr-6 and Leu-8 for Ser and Phe were found. Ornitho-kinin induced a hypotension on chicken and contracted the isolated smooth muscle. However, it did not any effect on the isolated rat uterus, suggesting that the specificity may be due to replacement of Phe-8 by Leu. The NH2-terminal 30 amino acid residues of ornitho-kininogen exhibited 43 % identity with that of bovine kininogen.

Hog pancreatic α-amylase. Preparation and characterization

1979 ◽  
Vol 44 (1) ◽  
pp. 288-293 ◽  
Author(s):  
Ivan Kluh
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Disulfide Bonds ◽  
Polypeptide Chain ◽  
Deae Cellulose ◽  
Amino Acid Residues ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
End Group

Crystalline α-amylase (EC 3.2.1.1) was prepared from hog pancreas. The preparation obtained was resolved into two isozymes by chromatography on DEAE-cellulose. The molecular weight (51 500), amino acid composition, and terminal groups of both isozymes were determined. Both isozymes have a single polypeptide chain containing 460-465 amino acid residues. The amino acid composition of both isozymes is similar. None of them has a free N-terminal end group. Both isozymes are C-terminated with leucine. The molecule of each isozyme is cross-linked by 5 disulfide bonds and contains two sulfhydryl groups.

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