Not More than Three Tissue Kallikreins Identified from Organs of the Guinea Pig
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F. Fiedler
Abstract
The large and varied multigene families of tissue kallikreins of rat and mouse are considered to selectively release as many bioactive peptides. In order to determine whether a similar family of enzymes is expressed in the organs of the guinea pig purification studies were performed. Tissue kallikreins from the submandibular gland, coagulating gland/prostate complex and the pancreas were separated by affinity chromatography on benzamidine-Sepharose. Amino-terminal sequences, the patterns of hydrolysis rates of a number of peptide p-nitroanilides, inactivation rates by active site-directed irreversible inhibitors, specific kininogenase activities and types of kinin released were used to probe the identity of the isolated enzymes.
Guinea pig tissue kallikreins 1 and 2 have been reported previously. In the present study we have identified a third type, designated tissue kallikrein 1a because of its sequence similarity to kallikrein 1, which differs from the latter in the catalytic properties. The inferred occurrence of not more than two or three independent tissue kallikrein genes in the guinea pig contrasts with the varied family of enzymes expressed by the large number of such genes present in rats and mice. Expression in the guinea pig (and also in humans) of only a small number of tissue kallikreins makes specific processing of a multitude of biologically active peptides by such enzymes unlikely.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- To Our Authors, Readers and Subscribers. Biological Chemistry 1999 - Increased Page Number and Online Accessibility
- Proto-Oncogenes, Unlike Harmless Genes, Tend to Be Dispersed in the Human Genome: Selection Against Out-of-Register Recombination?
- The Human H2A and H2B Histone Gene Complement
- Efficient Control of raf Gene Expression by CAP and Two Raf Repressors that Bend DNA in Opposite Directions
- Molecular Models of Acidic PePtides From Pea Bud Chromatin And Seminal Plasma. Divalent Cations-Mediated Interaction With Dna
- Cytidine Triphosphate Synthase Activity and mRNA Expression in Normal Human Blood Cells
- Studies with Lysine N6-Hydroxylase. Effect of a Mutation in the Assumed FAD Binding Site on Coenzyme Affinities and on Lysine Hydroxylating Activity
- The Recombinant Thermosome from the Hyperthermophilic Archaeon Methanopyrus kandleri: In Vitro Analysis of Its Chaperone Activity
- Not More than Three Tissue Kallikreins Identified from Organs of the Guinea Pig
- Activation of Protein C by Arginine-Specific Cysteine Proteinases (Gingipains-R) from Porphyromonas gingivalis
- Alteration of Mosaic Methylation of the Repeat Unit of the Human Ribosomal RNA Genes in Lung Cancer
- Degradation of the Cyclic AMP Antagonist Prostaglandylinositol Cyclic Phosphate (Cyclic PIP) by Dephosphorylation
- Homo-Dimeric Spherulin 3a: A Single-Domain Member of the bg-Crystallin Superfamily
- cDNA Sequencing of Guinea Pig a2-HS Glycoprotein, Its Expression in Various Tissues and Acute Phase Expression
- Phage Display Selection of P1 Mutants of BPTI Directed against Five Different Serine Proteinases
