The Biological Activity of α-1-Antichymotrypsin: The Change of Chymotrypsin-Inhibitory and Immunoenhancing Activities by Heat Treatment

The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-I-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C, 55°C or 60°C for 15 min. It was found that antichymotryptic activity was reduced by half when α-1-antichymotrypsin was heated at 55°C and was n...

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Published inJournal of biochemistry (Tokyo) Vol. 92; no. 6; pp. 1979 - 1983
Main Authors MATSUMOTO, Masahiko, YAMAMURA, Masaichi, TSUDA, Michio, TAKADA, Shigeo, KATSUNUMA, Tsunehiko
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.01.1982
The Japanese Biochemical Society
Subjects
Online AccessGet full text
ISSN0021-924X
DOI10.1093/oxfordjournals.jbchem.a134129

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Abstract The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-I-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C, 55°C or 60°C for 15 min. It was found that antichymotryptic activity was reduced by half when α-1-antichymotrypsin was heated at 55°C and was not detected at all when heating was carried out at 60°C. α-1-Antichymotrypsin which was heated at 60°C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated α-1-antichymotrypsin on antibody response was studied in mice. α-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60°C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60°C. In single radial immunodiffusion analysis, α-1-anti-chymotrypsin did not form a halo after being heated at 60°C. In conclusion, when α-1-antichymotrypsin was heated at 60°C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.
AbstractList The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-I-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C, 55°C or 60°C for 15 min. It was found that antichymotryptic activity was reduced by half when α-1-antichymotrypsin was heated at 55°C and was not detected at all when heating was carried out at 60°C. α-1-Antichymotrypsin which was heated at 60°C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated α-1-antichymotrypsin on antibody response was studied in mice. α-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60°C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60°C. In single radial immunodiffusion analysis, α-1-anti-chymotrypsin did not form a halo after being heated at 60°C. In conclusion, when α-1-antichymotrypsin was heated at 60°C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-1-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C, 55°C or 60°C for 15min. It was found that antichymotryptic activity was reduced by half when α-1-antichymotrypsin was heated at 55°C and was not detected at all when heating was carried out at 60°C. α-1-Antichymotrypsin which was heated at 60°C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated α-1-antichymotrypsin on antibody response was studied in mice. α-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60°C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60°C. In single radial immunodiffusion analysis, α-1-antichymotrypsin did not form a halo after being heated at 60°C. In conclusion, when α-1-antichymotrypsin was heated at 60°C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha-1-antichymotrypsin was studied. alpha-1-Antichymotrypsin was treated at 50 degrees C, 55 degrees C or 60 degrees C for 15 min. It was found that antichymotryptic activity was reduced by half when alpha-1-antichymotrypsin was heated at 55 degrees C and was not detected at all when heating was carried out at 60 degrees C. alpha-1-Antichymotrypsin which was heated at 60 degrees C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated alpha-1-antichymotrypsin on antibody response was studied in mice. alpha-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60 degrees C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60 degrees C. In single radial immunodiffusion analysis, alpha-1-antichymotrypsin did not form a halo after being heated at 60 degrees C. In conclusion, when alpha-1-antichymotrypsin was heated at 60 degrees C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha-1-antichymotrypsin was studied. alpha-1-Antichymotrypsin was treated at 50 degrees C, 55 degrees C or 60 degrees C for 15 min. It was found that antichymotryptic activity was reduced by half when alpha-1-antichymotrypsin was heated at 55 degrees C and was not detected at all when heating was carried out at 60 degrees C. alpha-1-Antichymotrypsin which was heated at 60 degrees C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated alpha-1-antichymotrypsin on antibody response was studied in mice. alpha-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60 degrees C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60 degrees C. In single radial immunodiffusion analysis, alpha-1-antichymotrypsin did not form a halo after being heated at 60 degrees C. In conclusion, when alpha-1-antichymotrypsin was heated at 60 degrees C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha-1-antichymotrypsin was studied. alpha-1-Antichymotrypsin was treated at 50 degrees C, 55 degrees C or 60 degrees C for 15 min. It was found that antichymotryptic activity was reduced by half when alpha-1-antichymotrypsin was heated at 55 degrees C and was not detected at all when heating was carried out at 60 degrees C. alpha-1-Antichymotrypsin which was heated at 60 degrees C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated alpha-1-antichymotrypsin on antibody response was studied in mice. alpha-1-Antichymotrypsin increased the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60 degrees C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes. Circular dichroism in the region of side chain absorption showed that the intensities of the spectra at 296, 284, and 265 nm decreased with a rise in temperature from 50 to 60 degrees C. In single radial immunodiffusion analysis, alpha-1-antichymotrypsin did not form a halo after being heated at 60 degrees C. In conclusion, when alpha-1-antichymotrypsin was heated at 60 degrees C, the immunoenhancing activity remained intact while the antichymotryptic activity was lost with the conformational change.
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha -1-antichymotrypsin was studied. alpha -1-Antichymotrypsin was treated at 50 degree C, 55 degree C or 60 degree C for 15 min. It was found that antichymotryptic activity was reduced by half when alpha -1-antichymotrypsin was heated at 55 degree C. alpha -1-Antichymotrypsin which was heated at 60 degree C did not form a complex with chymotrypsin, but became a substrate for chymotrypsin. The effect of native and heated alpha -1-antichymotrypsin on antibody response was studied in mice. alpha -1-Antichymotrypsin increassed the number of anti-sheep erythrocytes antibody producing cells even when it was heated at 60 degree C. Circular dichroism and single radial immunodiffusion were used to detect conformational changes.
Author TSUDA, Michio
YAMAMURA, Masaichi
TAKADA, Shigeo
MATSUMOTO, Masahiko
KATSUNUMA, Tsunehiko
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1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, and a Tokai medical research grant, Japan.
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Snippet The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-I-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C,...
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of α-1-antichymotrypsin was studied. α-1-Antichymotrypsin was treated at 50°C,...
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha-1-antichymotrypsin was studied. alpha-1-Antichymotrypsin was treated at...
The relationship between chymotrypsin-inhibitory and immunoenhancing activity of alpha -1-antichymotrypsin was studied. alpha -1-Antichymotrypsin was treated...
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SubjectTerms Adjuvants, Immunologic
alpha 1-Antichymotrypsin
Animals
Antibody Formation
C.D
Chymotrypsin - antagonists & inhibitors
Chymotrypsin - metabolism
Chymotrypsin - pharmacology
Hot Temperature
Immunodiffusion
immunostimulation
Male
Mice
Mice, Inbred BALB C
Protein Conformation
thermal stability
Title The Biological Activity of α-1-Antichymotrypsin: The Change of Chymotrypsin-Inhibitory and Immunoenhancing Activities by Heat Treatment
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