Human trypsin

Reseland, J.E., et al. 1996. Proteinase inhibitors induce selective stimulation of human trypsin and chymotrypsin secretion. J Nutr 126 634. 

Yousef GM, Elliott MB, Kopolovic AD, Serry E, Diamandis EP. Sequence and evolutionary analysis of the human trypsin subfamily of serine peptidases. Biochim Biophys Acta 2004 1698 77-86. 

Cystic fibrosis is a lethal autosomal recessive disorder in Caucasians, with an incidence of 1 2000 in the general population. Newborn babies with this disease have increased serum trypsin concentrations. Thus, Crossley et al. developed a radioimmunoassay for human trypsin in dried blood samples on filter paper and used it for neonatal screening for this disease (C9). A non-isotopic immunoassay, such as enzyme immunoassay of trypsin, will be developed for this purpose. 

Raehs SC, Sandow J, Wirth K, Merkle HP (1988) The adjuvant effect of bacitracin on nasal absorption of gonadorelin and buserelin in rats. Pharm Res 5 689-693 Ramon J, Saez V, Baez R, Aldana R, Hardy E (2005) PEGylated Interferon-alpha2b A Branched 40K Polyethylene Glycol Derivative. Pharm Res 22 1375-1387 Reseland JE, Holm H, Jacobsen MB, Jenssen TG, Hanssen LE (1996) Proteinase inhibitors induce selective stimulation of human trypsin and chymotrypsin secretion. J Nutr 126 634-642... 

Corn Seed-derived Recombinant Human Trypsin to Repiace Bovine Pancreas-derived Trypsin... 

Reseland, J. E., Holm, H., Jacobsen, M. B., Jenssen, T. G. and Hanssen, L. E., Proteinase inhibitors induce selective stimulation of human trypsin and chy-mobyp>sin secretion. Hum. Clin. Nutr., 126, 634,1996. 

Inhibitor activity is normally determined with commercial animal enzymes, e. g., bovine trypsin or bovine chymotrypsin. The evaluation of a potential effect of the inhibitors on human health assumes that the inhibition of human enzymes is known. Present data show that inhibitors from legumes generally inhibit human trypsin to the same extent or a little less than bovine trypsin. On the other hand, human chymotrypsin is inhibited to a much greater extent by most legumes. Ovomucoid and ovoinhibitor from egg white as well as the Kazal inhibitor from bovine pancreas do not inhibit the human enzymes. The Kunitz inhibitor from bovine pancreas inhibits human trypsin but not chymotrypsin. The data obtained greatly depend not only on the substrate used, but also on the enzyme preparation and the reaction conditions, e. g., on the ratio enzyme/inhibitor. The stability of an inhibitor as it passes through the stomach must also be taken into account in the evaluation of a potential effect (cf. Table 16.15). The Kunitz inhibitor of soybeans, for... 

Lupine seed, though used primarily in animal feeds (see Feeds AND FEED ADDITIVES), does have potential for use in human appHcations as a replacement for soy flour, and is reported to contain both trypsin inhibitors and hemagglutenins (17). The former are heat labile at 90°C for 8 minutes the latter seem much more stable to normal cooking temperatures. Various tropical root crops, including yam, cassava, and taro, are also known to contain both trypsin and chymotrypsin inhibitors, and certain varieties of sweet potatoes may also be impHcated (18). 

Pea.nuts, The proteins of peanuts are low in lysine, threonine, cystine plus methionine, and tryptophan when compared to the amino acid requirements for children but meet the requirements for adults (see Table 3). Peanut flour can be used to increase the nutritive value of cereals such as cornmeal but further improvement is noted by the addition of lysine (71). The trypsin inhibitor content of raw peanuts is about one-fifth that of raw soybeans, but this concentration is sufficient to cause hypertrophy (enlargement) of the pancreas in rats. The inhibitors of peanuts are largely inactivated by moist heat treatment (48). As for cottonseed, peanuts are prone to contamination by aflatoxin. FDA regulations limit aflatoxin levels of peanuts and meals to 100 ppb for breeding beef catde, breeding swine, or poultry 200 ppb for finishing swine 300 ppb for finishing beef catde 20 ppb for immature animals and dairy animals and 20 ppb for humans. 

Look up the structure of human insulin (Section 26.7), and indicate w here in each chain the molecule is cleaved by trypsin and chymotrypsin. 

PA S1 S01.258 Trypsin-2 (human-type) Potential use in detection of acute panreatitis... 

These authors also mention some shortcomings that should be borne in mind, in particular, that some peptides observed were from the autolysis of trypsin, the digestion agent, and from contaminants such as human keratin, while some peptide ions did not produce interpretable MS-MS spectra. 

Matthews DA, Smith WW, Ferre RA, Condon B, Budahazi G, Sisson W, Villafranca JE, Janson CA, McElroy HE, Gribskov CL et al (1994) Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein. CeU 77 761-771... 

Figure 42-12. Structure of human proinsulin. Insulin and C-peptide molecules are connected at two sites by dipeptide links. An initial cleavage by a trypsin-like enzyme (open arrows) followed by several cleavages by a car-boxypeptidase-like enzyme (solid arrows) results in the production of the heterodimeric (AB) insulin molecule (light blue) and the C-peptide.

Irreversible inhibition is probably due to the alkylation of a histidine residue.43 Chymotrypsin is selectively inactivated with no or poor inhibition of human leukocyte elastase (HLE) with a major difference the inactivation of HLE is transient.42,43 The calculated intrinsic reactivity of the coumarin derivatives, using a model of a nucleophilic reaction between the ligand and the methanol-water pair, indicates that the inhibitor potency cannot be explained solely by differences in the reactivity of the lactonic carbonyl group toward the nucleophilic attack 43 Studies on pyridyl esters of 6-(chloromethyl)-2-oxo-2//-1 -benzopyran-3-carboxylic acid (5 and 6, Fig. 11.5) and related structures having various substituents at the 6-position (7, Fig. 11.5) revealed that compounds 5 and 6 are powerful inhibitors of human leukocyte elastase and a-chymotrypsin thrombin is inhibited in some cases whereas trypsin is not inhibited.21... 

Nielsen, R. G., Riggin, R. M., and Rickard, E. C., Capillary zone electrophoresis of peptide fragments from trypsin digestion of biosynthetic human growth hormone, /. Chromatogr., 480, 393, 1990. 

Boldicke, T., Kindt, S., Maywald, F., Fitzlaff, G., Bocher, M., Frank, R., and Collins, J. (1988) Production of specific monoclonal antibodies against the active sites of human pancreatic secretory trypsin inhibitor variants by in vitro immunization with synthetic peptides. Eur. J. Biochem. 175, 259-264. 

As indicated in Table 2.1, most of the promoters used in plant tissue culture have been based on the constitutive cauliflower mosaic virus (CaMV) 35S promoter. In contrast, inducible promoters have the advantage of allowing foreign proteins to be expressed at a time that is most conducive to protein accumulation and stability. Although a considerable number of inducible promoters has been developed and used in plant culture applications, e.g. [32-37], the only one to be applied thus far for the production of biopharmaceutical proteins is the rice a-amylase promoter. This promoter controls the production of an a-amylase isozyme that is one of the most abundant proteins secreted from cultured rice cells after sucrose starvation. The rice a-amylase promoter has been used for expression of hGM-CSF [10], aranti-trypsin [12, 29, 38, 39] and human lysozyme [30]. 

CP coat protein CtxB cholera toxin B subunit scFv single chain Fv antibody fragment TMOF trypsin modulating oostatic factor MAB monoclonal antibody GFP green fluorescent protein CPV Canine parvovirus BHV Bovine herpes virus FMDV Foot and mouth disease virus HCV Hepatitis C virus HRV Human rhino Virus MEV Mink enteritis virus MHV Murine hepatitis virus MV Measles virus RSV Respiratory syncytial virus... 

---