Heterochromatin and cytogenetic polymorphisms in Cebus apella (Cebidae,Platyrrhini)

Cytogenetic studies have been carried out in 39 specimens of C. apella of different origins. Three different morphologies, one affecting the long arm of chromosome 4 and two affecting pair 17, have been detected. In each case, they can be related by paracentric inversions. Heterochromatin polymorphisms affecting terminal or interstitial C+ regions have also been observed. The length of the terminal heterochromatic region in the long arms of chromosome 11 is variable in C. apella sp., in C. a. paraguayanus and absent in the C. a. nigritus specimens studied. Interstitial C + bands can be observed in the long arms of the biarmed chromosomes 4 and 6, and in the long arms of the acrocentric pairs 12, 13, 17, 18, 19, 20, and 21. Interstitial C + bands in the long arms of chromosomes 4, 12, 17, and 19 are present in all animals studied, although their size is variable, especially in the case of chromosomes 17 and 19. © 1995 Wiley-Liss, Inc.     

The major locus for multifactorial nonsyndromic cleft lip maps to mouse Chromosome 11

Cleft lip with or without cleft palate, CL(P), a common human birth defect, has a genetically complex etiology. An animal model with a similarly complex genetic basis is established in the A/WySn mouse strain, in which 20% of newborn have CL(P). Using a newly created congenic strain, AEJ.A, and SSLP markers, we have mapped a major CL(P)-causing gene derived from the A/WySn strain. This locus, here named clf1 (cleft lip) maps to Chromosome (Chr) 11 to a region having linkage homology with human 17q21-24, supporting reports of association of human CL(P) with the retinoic acid receptor alpha (RARA) locus.     

Purification and properties of the endocellular β-glucosidase of Candida cacaoi Buckley and Van Uden CBS 2020

D. DRIDER, P. POMMARES, P. CHEMARDIN, A. ARNAUD AND P. GALZY. 1993. The endocellular enzyme β-glucosidase of Candida cacaoi was purified by ion-exchange chromatography and gel filtration. The molecular weight was 220 ± 10 kDa; its optimum pH was between 4 and 5.5 and its optimum temperature was 60C. This enzyme was active against soluble glucosides tested with β(1–2), β(1–3), β(1–4) and even α(1–4) and α(1–6) and was inhibited by D-glucono-δ-lactone. The enzyme was constitutive but its synthesis was repressed by glucose.