Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tuberculin purified protein derivative (PPD) obtained from the filtrate of Mycobacterium tuberculosis was hydrolysed with proteinase, trypsin, or chymotrypsin. Each hydrolysate consisted of a tuberculin peptides mixture (TPM). From each TPM 16 fractions were obtained by ion-exchange chromatography on Dowex 50W-X8 but only one fraction was isolated from each of the 16 fractions which showed tuberculin activity in guinea pigs sensitized with M. bovis (bcg) or M. tuberculosis. This fraction was designated "purified tuberculin peptide" (PTP). The PTP fraction from the proteinase hydrolysate (PTP-proteinase) was rechromatographed on Dowex 1-X2 and two tuberculin peptide fractions having molecular weights of 3200 and 12,000 were isolated. The potency of these two fractions was assessed in guinea pigs sensitized with M. bovis (BCG) and with M. tuberculosis and they were approximately 4 to 7 times more potent than either the international standaCG and of at least equal potency to either PPD-S or Connaught PPD in guinea pigs sensitized with either M. kansasii, M. scrofulaceum, M. intracellulare, or M. avium whereas very little if any cross-reactivity was elicited by these two fractions. This lack of response indicates that either fraction could be used as an aid to differentiate between sensitization due to M. tuberculosis or M. bovis and sensitization attributed to other mycobacteria.
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PMID:Isolation of tuberculin peptides from tuberculin purified protein derivative (PPD). 10 8

BCG cell walls contain approximately 30% free lipids like other mycobacterial cell walls. The insoluble skeleton of the cell wall is made up of two covalently linked polymers, a peptidoglycan and an arabinogalactan mycolate, with which are associated non peptidoglycan amino acids and a glucan. We present data on two structural features: 1. The "non peptidoglycan" amino acids; they form two kinds of compounds: peptide chains which can be solubilized by proteolytic enzymes and a trypsin-chymotrypsin insensitive poly-alpha-L-glutamic acid. 2. Presence of meso-DAP-meso-DAP1) interpeptide linkages in the peptidoglycan: this new type represents at least 50% of the interpeptide linkages of the cell wall of the BCG strain.
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PMID:Chemical structure of the cell wall of Mycobacterium tuberculosis var. bovis, strain BCG. 12 48

Supernatants from spleen cells, derived from mice injected with BCG and cultured with PPD, specificially inhibited the migration of normal mouse peritoneal macrophages when compared with control supernatants. Migration inhibitory supernatants were also shown to decrease the detachment of adherent macrophages in a novel test system. Both macrophage migration and detachment inhibitory activities were abrogated by neuraminidase and chymotrypsin treatment of supernatants but were thermostable, suggesting that the detachment test is a sensitive index of MIF activity.
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PMID:Effects of migration inhibiting factor(s) on the in vitro detachment of macrophages. 110 Jul 29

The zeta potential of washed Tice substrain BCG organisms was measured over a range of ionic strengths from I = 0.005 to 0.1 M. No change in the isoelectric point of 3.4-3.7 was evident. Proteolytic enzymes (trypsin/chymotrypsin, pepsin, papain and pronase) and fluorodinitrobenzene abolished the cationic charge, suggesting that this is substantially due to amino groups associated with protein. Neither hot HCI nor cold trichloroacetic acid affected the charge, indicating that ionic groups are not associated with extractable polysaccharides. Methanolysis, treatment with HF and carbodiimide, and cationic detergent (cetyltrimethylammonium bromide) binding indicated that the negative charge was provided by carboxylic acids, phosphoesters and strong acidic groups, possibly sulphates. Standardless quantitative X-ray microanalysis revealed the presence of phosphorus and sulphur on the surface of actively growing BCG colonies.
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PMID:Origins of BCG surface charge: effect of ionic strength and chemical modifications on zeta potential of Mycobacterium bovis BCG, Tice substrain, cells. 140 39

Sera from mice which have been vaccinated with BCG and challenged with old tuberculin contain gamma interferon. These same sera also express antibacterial activity. Using Staphylococcus aureus we demonstrated that its growth was inhibited at dilutions of sera as high as 1:320. A 4% concentration of sera reduced the growth rate of the S. aureus from 1.6 to 0.6 doubling times per hour. The activity was stable at 56 degrees C but destroyed by 80 degrees C. It was nondialysable and destroyed by acid conditions (pH 2.0) and by the proteolytic enzymes trypsin and chymotrypsin. Antibodies to gamma interferon neutralized the antiviral activity but not the antibacterial activity. Mitogen-induced and virus-induced interferons did not have activity. We subsequently demonstrated that the factor could be induced in mice using BCG without the secondary old tuberculin challenge. No gamma interferon was found in the sera of mice given BCG without old tuberculin. These findings indicate that the antibacterial activity of these sera is not dependent on the presence of gamma interferon. We will continue to work to characterize and identify the antibacterial component in these sera.
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PMID:Antibacterial activity of BCG-induced, interferon-containing sera. 308 10