scholarly journals Bovine ß-Lactoglobulin E, F and G of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

1981 ◽  
Vol 34 (2) ◽  
pp. 133 ◽  
Author(s):  
K Bell ◽  
HA McKenzie ◽  
DC Shaw
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Tryptic Peptide ◽  
Bos Taurus ◽  
Peptide Mapping ◽  
Northern Territory ◽  
Aureus Strain ◽  
Residue Substitution ◽  
Additional Charge

An electrophoretic examination is made of samples of milk from eight Bali (banteng) cattle, Bos (Bibos) javanicus, in the Northern Territory of Australia. There are two new electrophoretically distinct bovine ft-Iactoglobulins, designated E and F, present in these samples. It is shown by amino acid analysis and tryptic peptide mapping of isolated samples that: (I) both E and F differ from the B variant of domestic cattle (Bos taurus) by + 1 G1y, -1 Glu at residue 157 or 158; and (2) the F variant has the additional charge differences from E and B due to + I Tyr, -1 Asp at residue 129 or 130. It is also shown by studies of peptides produced by the action of Staphylococcus aureus strain V8 protease and by more recent amino acid analyses that (1) the GlyjGlu substitution is at residue 158; (2) there is an additional Bali variant, designated ft-lactoglobulin G, differing from E by + 1 Met, -1 lie at residue 78, but having the same mobility as E; and (3) there is an hitherto undetected neutral residue substitution of + 1 Ser, -1 Pro at position 50 in the F variant. The relation of these variants to other known ft-lactoglobulin variants of the Bos genus is discussed.

scholarly journals Trypsin-catalysed formation of pig des-(23-63)-proinsulin from desoctapeptide-(B23-30)-insulin

1986 ◽  
Vol 234 (3) ◽  
pp. 665-670 ◽  
Author(s):  
T Kubiak ◽  
D Cowburn
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Receptor Binding ◽  
Amino Acid Analysis ◽  
Peptide Bond ◽  
Dimethyl Sulphoxide ◽  
Tris Buffer ◽  
Binding Ability ◽  
Solvent Systems

Incubation of pig desoctapeptide-(B23-30)-insulin with trypsin in solvent systems consisting of dimethyl sulphoxide, butane-1,4-diol and Tris buffer resulted in the formation of an extra peptide bond between Arg-B22 and Gly-A1 in the DOPI molecule. This DOPI derivative can also be regarded as pig des-(23-63)-proinsulin. The structure of the new, previously unreported, proinsulin analogue was determined on the basis of amino acid analysis, dansylation and digestion with Staphylococcus aureus V8 proteinase. Receptor-binding ability of des-(23-63)-proinsulin was 20% of that of pig desoctapeptide-(B23-30)-insulin and 0.02% of that of pig insulin.

scholarly journals A study of the subunit structure and the thiol reactivity of bovine liver uridine diphosphate glucose dehydrogenase

1972 ◽  
Vol 129 (4) ◽  
pp. 821-830 ◽  
Author(s):  
P. A. Gainey ◽  
T. C. Pestell ◽  
C. F. Phelps
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Peptide Mapping ◽  
Ph Dependence ◽  
Glucose Dehydrogenase ◽  
Group Analysis ◽  
Subunit Structure ◽  
Uridine Diphosphate ◽  
Thiol Groups ◽  
Thiol Reactivity

1. The amino acid analysis of UDP-glucose dehydrogenase is reported. 2. N-Terminal-group analysis indicates only one type of N-terminal amino acid, methionine, to be present. 3. Peptide ‘mapping’ in conjunction with the amino acid analysis indicates that the subunits of the enzyme are similar if not identical. 4. The various kinetic classes of thiol group were investigated by reaction with 5,5′-dithiobis-(2-nitrobenzoate). 5. NAD+, UDP-glucose and UDP-xylose protect the two rapidly reacting thiol groups of the hexameric enzyme. 6. Inactivation of the enzyme with 5,5′-dithiobis-(2-nitrobenzoate) indicates the involvement of six thiol groups in the maintenance of enzymic activity. 7. The pH-dependence of UDP-xylose inhibition of the enzyme was investigated. 8. The group involved in the binding of UDP-xylose to the protein has a heat of ionization of about 33kJ/mol and a pK of 8.4–8.6. 9. It is suggested that UDP-xylose has a cooperative homotropic effect on the enzyme.

NUCLEOTIDE SEQUENCE OF THE STAPHYLOCOAGULASE GENE FROM STAPHYLOCOCCUS AUREUS STRAIN BB

1987 ◽  
Author(s):  
S Kaida ◽  
T Miyata ◽  
S Kawabata ◽  
T Morita ◽  
Y Yoshizawa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Tandem Repeats ◽  
Molar Ratio ◽  
Clotting Factor ◽  
Aureus Strain ◽  
Activation Process ◽  
Coding Region ◽  
Flanking Region

Staphylocoagulase (SC) is a secretary protein produced by several strains of Staphylococcus aureus (S. aureus). This protein forms a molecular complex ("staphylothrombin") with human prothrombin in a molar ratio of 1:1. The complex displays the ability to clot fibrinogen and to hydrolyze the synthetic tripeptide substrates for α-thrombin. The formation of staphylothrombin does not require proteolytic cleavage of the prothrombin molecule, and this mechanism differs markedly from the activation process by either blood-clotting factor Xa or snake venom procoagulant.In the present studies, a pAT153 library containing partial Mbo I-digested DNA prepared from aureus strain BB has been screened with a fibrin gel formation method. The identity of these clones with SC was confirmed by DNA sequence analysis and by comparison of the derived amino acid sequence with that determined for the purified SC protein. One of the positive colonies was isolated and 3.1 Kb of the insert DNA was determined by the dideoxy chain termination method. The results indicated that the insert DNA consists of 148 bp 5' flanking region, protein coding region of 715 amino acids and 746 bp 3' flanking region, and that SC from strain BB is synthesized as a precursor with a signal peptide of 26 amino acids. Thus, the mature form was composed of 689 amino acids with a molecular weight of 77,337- The NH2-terminal sequence (324 amino acids) of SC isolated from S. aureus strain 213 (S. Kawabata et al. (1986): J. Biol. Chem. 261, 527-531) was compared with that of SC derived from strain BB. The sequence homology between them was found to show 57 %. It was also found that SC derived from strain BB was composed of 8 tandem repeats (27 amino acid residues in length) in the COOH-terminal region, although their functions are not known.

Phosphofructokinase from Escherichia coli: Further evidence for identical subunits

1978 ◽  
Vol 56 (8) ◽  
pp. 836-838 ◽  
Author(s):  
Bruce N. Thornburgh ◽  
Licia Liu Wu ◽  
Charles C. Griffin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Affinity Chromatography ◽  
Tryptic Peptide ◽  
Peptide Mapping

A procedure for the purification of Escherichia coli phosphofructokinase by affinity chromatography is described. The results of amino acid analyses of the purified protein and tryptic peptide mapping suggest that the tetrameric phosphofructokinase is composed of chemically identical subunits. In addition, the reaction product, ADP, was observed to bind to 4.1 ± 0.1 equal and independent sites on the enzyme.

scholarly journals The subunit structure of rabbit skeletal-muscle phosphofructokinase and the amino acid sequence of the tryptic peptide containing the highly reactive thiol group

1977 ◽  
Vol 163 (2) ◽  
pp. 309-316 ◽  
Author(s):  
I A Simpson ◽  
M R Hollaway ◽  
J Beard
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tryptic Peptide ◽  
Peptide Mapping ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Class I ◽  
Subunit Structure

1. The single highly reactive (class I) thiol group per 80000-mol.wt. subunit of skeletal-muscle phosphofructokinase was specifically carboxymethylated with iodo[2-14C]acetate, and after denaturation the remaining thiol groups were carboxymethylated with bromo[2-3H]acetate. After tryptic digestion and peptide ‘mapping’ it was found that the 14C radioactivity was in a spot that did not contain significant amounts of 3H radioactivity, so it is concluded that there is not a second, ‘buried’ cysteine residue within a sequence identical with that of the class-I cysteine peptide. 2. The total number of tryptic peptides as well as the number of those containing cysteine, histidine or tryptophan were inconsistent with the smallest polypeptide chain of phosphofructokinase (mol.wt. about 80000) being composed of two identical amino acid sequences. 3. The amino acid sequence of the tryptic peptide containing the class-I thiol group was shown to be Cys-Lys-Asp-Phe-Arg. This sequence is compared with part of the sequence containing the highly reactive thiol group of phosphorylase.

Purification of the delta toxin of Staphylococcus aureus

1970 ◽  
Vol 16 (8) ◽  
pp. 703-708 ◽  
Author(s):  
J. D. Caird ◽  
G. M. Wiseman
Keyword(s):  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Ammonium Sulphate ◽  
Deae Cellulose ◽  
Aureus Strain ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Two Peaks

An improved procedure for the purification of the delta toxin of Staphylococcus aureus strain E-delta has been devised which relies upon precipitation at pH 4.0 and further treatment with ammonium sulphate. A final step consists of passage twice through a column of DEAE-cellulose. Toxin obtained by this method appeared to be homogeneous on the basis of immunodiffusion and electrophoresis studies. However, two peaks with sedimentation coefficients of 2.8 S and 9.8 S were obtained when toxin was examined in the ultracentrifuge. Proline was identified as the N-terminal amino acid. No other N-terminal amino acids were detected in the purified toxin.

Amino acid analysis and peptide mapping of bovine carotid actin

1969 ◽  
Vol 175 (1) ◽  
pp. 165-173 ◽  
Author(s):  
Cecile Gosselin-Rey ◽  
Charles Gerday ◽  
Annie Gaspar-Godfroid ◽  
Mary E. Carsten
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Peptide Mapping
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