Abstract:
Agent for the detection of esterolytic and/or proteolytic enzymes, containing (a) an amino acid ester or peptide ester of a phenol, as the chromogenic enzyme substrate, and (b) a substance which accelerates the enzymatic cleavage of the amino acid ester or peptide ester bond of component (a), characterized in that it contains a polyamino acid with a molecular weight of between 1,000 and 2,000,000 as the accelerating substance.
Abstract:
Peptide derivatives of formula ##STR1## wherein R.sup.1 represents a substituted amino group which is capable of being split off enzymatically with formation of a colored or fluorescent compound R.sup.1 -H. The said peptide derivatives are used for quantitatively assaying the enzyme C.sub.1 -esterase. The assaying is carried out by reacting a medium which contains C.sub.1 -esterase or in which the latter is formed or consumed with a peptide derivative as defined above and measuring photometrically, spectrophotometrically, fluorescence-spectrophotometrically or electrochemically the quantity of split product R.sup.1 -H released per time unit by the catalytic hydrolytic action of the said enzyme on the peptide derivative.
Abstract:
Compounds which are substrates for mammalian enzymes, especially proteolytic and peptidase enzymes, are disclosed. These compounds, in general, have the general formula X-T, W-Y or X-(Pep)-Y, wherein X is a radiolabelled benzoyl or hydroxyphenylpropanoyl group, T is the --NH residue of a known chromogenic or fluorogenic substrate comprising at least one amino acid group which may be substituted with other organic groups, Y is a radiolabelled benzylamine group, W is the ##STR1## residue of a known chromogenic or fluorogenic substrate comprising at least one amino acid group which may be substituted with other organic groups, and (Pep) is a difunctional or polyfunctional residue from a known chromogenic or fluorogenic substrate comprising at least two amino acid groups in peptide linkage, which residue may be substituted with other organic groups. These substrates exhibit many advantages over the chromogenic and fluorogenic analogs, including greater sensitivity, surprising and unpredictable affinity and specificity, and the like.
Abstract:
What are disclosed are chromogenic peptides useful as substrates for the detection and determination of enzymes having a hydrolytic action and methods for detecting and determining enzymes with such peptides.
Abstract:
Novel di-to heptapeptides representing fragments of the carboxyl terminal of thymosin .alpha..sub.1 are active as agents which affect regulation, differentiation and function of thymus dependent lymphocytes.
Abstract:
New peptides are disclosed which have biological activity of the same type as known calcitonins which have both a D-amino acid in position 24 instead of the natural L-amino acid and are substitution analogs of the natural calcitonins. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.
Abstract:
There are disclosed polypeptides having the formula:R-Arg-Lys-Asp-Val-D-Ala-R.sub.1whereinR is hydrogen, alkanoyl of 1-4 carbon atoms or aroyl of 6-10 carbon atoms; andR.sub.1 is amino, monoalkylamino of 1-4 carbon atoms, dialkylamino of 1-4 carbon atoms, hydroxy, alkoxy of 1-4 carbon atoms, ##STR1## the fully protected peptide-resin intermediates thereof, or pharmaceutically acceptable salts thereof. These polypeptides have the capability of inducing the differentiation of t-lymphocytes and thus are useful in a number of therapeutic areas.
Abstract:
An improved method is provided for detecting endotoxins in blood serum and/or plasma, particularly human blood fractions. The method employs king crab amebocyte lysate, preferably Limulus amebocyte lysate, in the presence of a substrate which has a selected colorimetric indicator bound to it. The indicator is capable of being split from the substrate by an enzyme which can be generated in the lysate by endotoxins in the blood. Thus, the endotoxins convert proenzyme in the lysate to the enzyme which effects the splitting off of the colorimetric indicator from the substrate. The endotoxin concentration in the blood can thus be determined colorimetrically, that concentration being proportional to the concentration of color indicator split from the substrate. The blood sample need not be extracted, as is required in prior methods, with a solvent such as chloroform to remove inhibitors therein which would interfere with a lysate gelation reaction. Heparin is utilized in the present method in a concentration sufficient to stabilize the lysate against loss of potency but insufficient to inhibit the reaction whereby endotoxin generates the described splitting enzyme from proenzyme in the lysate and the reaction of the enzyme to cause the split. The blood fraction need not be diluted with water and the lysate may be one which has been reconstituted from dry powder, if desired. The method is simple, highly effective, reproducible, inexpensive and rapid.
Abstract:
The polypeptides of the formula: ##STR1## in which R.sup.1 is hydrogen, methyl, allyl, cyclopropylmethyl, cyclobutylmethyl or Arg;R.sup.2 is hydrogen or methyl;R.sup.3 is hydrogen, (lower) alkylthio or a repeating unit of the depicted polypeptide forming a dimeric dithio ether;R.sup.4 is hydrogen or methyl;X is D-Ser, D-Thr, D-Asn, D-Asp, D-Gln, D-Glu, D-His, D-Lys, D-Arg, D-Leu and D-Met;and R.sup.5 represents hydroxyl, (lower) alkyl ester amide or (lower)alkyl amide of the 1-carboxyl group of the C-terminal amino acid or a --CH.sub.2 OH group replacing said 1-carboxyl group,or a pharmaceutically acceptable salt thereof, exert an analgesic effect in warm-blooded animals.