Sporidesmins. XIV. Modifications to the Opened -S-S- Bridge of Sporidesmin for Coupling to Proteins by Transacylation

1975 ◽  
Vol 28 (9) ◽  
pp. 2043 ◽  
Author(s):  
J Ronaldson
Keyword(s):  
Mass Spectrum ◽  
Serum Albumin ◽  
Thiol Group ◽  
Rabbit Serum ◽  
Amino Groups ◽  
Plasma Albumin ◽  
Bovine Plasma ◽  
Conventional Tests

Alkylation of the opened -S-S- bridge of sporidesmin formed diethyl secosporidesmin-S,S?-diacetate(3), dimethyl secosporidesmin-S,S?- diacetate (4), methyl 3-mercaptosecosporidesmin-11a-S-acetate (5) and methyl 11a-mercaptosecosporidesmin-3-S-acetate (6) which were condensed with ε-amino groups of poly(L-lysine), bovine plasma albumin and rabbit serum albumin. The thiol group in compound (6) could not be demonstrated by conventional tests but its presence was established by its mass spectrum.

PREPARATION OF AN ESTRONE–PROTEIN CONJUGATE

1958 ◽  
Vol 36 (11) ◽  
pp. 1177-1184 ◽  
Author(s):  
L. Goodfriend ◽  
A. H. Sehon
Keyword(s):  
Serum Albumin ◽  
Free Amino ◽  
Electrophoretic Analysis ◽  
Amino Derivative ◽  
Rabbit Serum ◽  
Amino Groups ◽  
Protein Conjugate ◽  
Lysine Residues ◽  
Albumin Molecule

A procedure is described for the preparation of an estrone–protein conjugate. The 17-amino derivative of estrone was prepared and converted by phosgenation to estrone-17-isocyanate. The latter was coupled to rabbit serum albumin. Ultraviolet analysis and determination of free amino groups of both albumin and estrone–albumin conjugate showed that the latter contained about 25 estrone residues per albumin molecule. Electrophoretic analysis provided additional evidence that coupling had occurred at the ε-amino groups of the lysine residues of albumin.

PREPARATION OF AN ESTRONE–PROTEIN CONJUGATE

1958 ◽  
Vol 36 (1) ◽  
pp. 1177-1184 ◽  
Author(s):  
L. Goodfriend ◽  
A. H. Sehon
Keyword(s):  
Serum Albumin ◽  
Free Amino ◽  
Electrophoretic Analysis ◽  
Amino Derivative ◽  
Rabbit Serum ◽  
Amino Groups ◽  
Protein Conjugate ◽  
Lysine Residues ◽  
Albumin Molecule

A procedure is described for the preparation of an estrone–protein conjugate. The 17-amino derivative of estrone was prepared and converted by phosgenation to estrone-17-isocyanate. The latter was coupled to rabbit serum albumin. Ultraviolet analysis and determination of free amino groups of both albumin and estrone–albumin conjugate showed that the latter contained about 25 estrone residues per albumin molecule. Electrophoretic analysis provided additional evidence that coupling had occurred at the ε-amino groups of the lysine residues of albumin.

scholarly journals o-Quinones formed in plant extracts. Their reaction with bovine serum albumin

1969 ◽  
Vol 112 (5) ◽  
pp. 619-629 ◽  
Author(s):  
W. S. Pierpoint
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Plant Extracts ◽  
Bovine Serum ◽  
Succinic Anhydride ◽  
Thiol Group ◽  
Excess Oxygen ◽  
Amino Group ◽  
Amino Groups ◽  
Ellman's Reagent

1. The reactions between chlorogenoquinone, the o-quinone formed during the oxidation of chlorogenic acid, and bovine serum albumin depend on the ratio of reactants. 2. When the serum albumin is in excess, oxygen is not absorbed and the products are colourless. This reaction probably involves the thiol group of bovine serum albumin; it does not occur with bovine serum albumin which has been treated with p-chloromercuribenzoate, iodoacetamide or Ellman's reagent. 3. When bovine serum albumin reacts with excess of chlorogenoquinone, oxygen is absorbed and the products are red. The red colour is probably formed by reaction of the lysine ∈-amino groups of bovine serum albumin, as it is prevented by treating the protein with formaldehyde, succinic anhydride or O-methylisourea. 4. Bovine serum albumin modified by a 1·5-fold (BSA-Q) and a fivefold (BSA-Q2) excess of chlorogenoquinone were separated by chromatography on DEAE-Sephadex A-50, and some of their properties observed. 5. Reaction of BSA-Q2 with fluorodinitrobenzene suggests that the terminal α-amino group, as well as lysine ∈-amino groups, are combined with chlorogenoquinone.

scholarly journals Mechanisms of heat damage in proteins

1970 ◽  
Vol 24 (1) ◽  
pp. 313-329 ◽  
Author(s):  
J. Bjarnason ◽  
K. J. Carpenter
Keyword(s):  
Amino Acids ◽  
Main Reaction ◽  
Amino Group ◽  
Amino Groups ◽  
Sulphur Compounds ◽  
Plasma Albumin ◽  
Small Loss ◽  
Bovine Plasma ◽  
Carboxylic Groups ◽  
Ammonia Liberation

1. Bovine plasma albumin (BPA) containing approximately 14% moisture, when heated for 27 h at 115° suffered an appreciable loss of cystine and a small loss of lysine; at 145° all the amino acids except glutamic acid and those with paraffin side-chains, showed considerable losses. Isoleucine also showed some loss through racemization to alloisoleucine.2. BPA heated at 115° evolved H2S; at 145° other sulphur compounds were released as well, all coming from the breakdown of cystine. Possible mechanisms for this are discussed.3. Ammonia was also liberated from BPA heated at 115°. The degree of correlation of lysine binding in different proteins with ammonia liberation and amide changes has led us to suggest that the main reaction of ε-amino lysine groups is with amide groups of asparagine and glutamine. Reaction of ε-amino groups with carboxylic groups is thought to be less important.4. Model experiments have shown that a reaction between amide groups and the e-amino group of lysine in proteins can occur at practical drying temperatures.5. Reactions of the ε-amino group of lysine with destruction products of cystine is also considered to be partially responsible for the lysine binding in heated proteins.

Bovine Platelet Proteins

1969 ◽  
Vol 21 (03) ◽  
pp. 409-418 ◽  
Author(s):  
S Łopaciuk ◽  
N. O Solum
Keyword(s):  
Bovine Serum ◽  
Protein Composition ◽  
Disc Electrophoresis ◽  
Plasma Fibrinogen ◽  
Plasma Albumin ◽  
Precipitin Line ◽  
Bovine Plasma ◽  
Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

scholarly journals An Endonuclease Associated with Bovine Plasma Albumin Fraction

1972 ◽  
Vol 247 (1) ◽  
pp. 193-198
Author(s):  
Motoaki Anai ◽  
Hiroyuki Haraguchi ◽  
Yasuyuki Takagi
Keyword(s):  
Plasma Albumin ◽  
Albumin Fraction ◽  
Bovine Plasma

The Relation of Free Sulfhydryl Groups to Chromatographic Heterogeneity and Polymerization of Bovine Plasma Albumin*

Biochemistry ◽  
1962 ◽  
Vol 1 (1) ◽  
pp. 60-68 ◽  
Author(s):  
Robert W. Hartley ◽  
Elbert A. Peterson ◽  
Herbert A. Sober
Keyword(s):  
Sulfhydryl Groups ◽  
Plasma Albumin ◽  
Bovine Plasma

CD-resolved secondary structure of bovine plasma albumin in acid-induced isomerization*

2009 ◽  
Vol 22 (3) ◽  
pp. 333-340 ◽  
Author(s):  
SEIICHI ERA ◽  
HIROSHI ASHIDA ◽  
SHUNJI NAGAOKA ◽  
HIROSHI INOUYE ◽  
MASARU SOGAMI
Keyword(s):  
Secondary Structure ◽  
Plasma Albumin ◽  
Bovine Plasma
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