田螺科五种螺的核型研究

以早期胚胎细胞为材料,用火焰干燥法制片,对分布于我国湖北省武汉市近郊的常见田螺科(Viviparidae)五种螺的核型进行了分析。结果:两种圆田螺的染色体数和国外报道的同一属的种类的一致。而三种环棱螺的染色体数,则较国外报道的另两种的少得多。在铜锈环棱螺的核型中,其m组的第一对和sm组的第四对染色体上,具有明显的随体,出现频率甚高。     

中国鲤科鱼类染色体组型的研究 Ⅱ.鲴亚科四种鱼的染色体组型

鲴亚科(Xenocyprininae)鱼类多为中小型鱼类,常见于江河湖泊等较宽阔的水域中,我国长江、黑龙江、黄河及珠江诸流域皆有分布,共有10种,隶属4个属(伍献文等,1964)。迄今尚未见有该亚科鱼类染色体组型的研究报道。本文是对其中三属四种鱼的染色体组型的观察结果。这四种鱼是银鲴(Xenocypris argentea)、黄尾鲴(Xenocypris davidi)、细鳞斜颌鲴(Plagiognathops microlepis)和逆鱼(Acanthobrama simoni)。其中黄尾鲴和细鳞斜颌鲴均为新的淡水养殖鱼(沈德长等,1981;陈楚星,1979)。     

Structural studies of an Inv (1, −2) kappa light chain

A Bence Jones protein with phenotype Inv (1, –2) was isolated from the urine of a patient with multiple myeloma. Inv typing of the patient's relatives established the presence of anInv ¹ allele in the kindred, and that the patient's genotype wasInv ¹/Inv ³. Hence, the absence of Inv (2) in the Bence Jones protein was shown to be genetic and not an artifact caused by the disease. The tryptic peptide-containing residues 191 through 194 were isolated and shown to be composed of Leu, Tyr, Ala, Cys, with Leu at the amino end. Hence, the residue at 191 is the same as that present in Inv (1, 2) Bence Jones proteins. More detailed study of the tryptic peptides established that residue 153 is Val rather than Ala as in all other K chains thus far studied. The primary sequence: Ala¹⁵³, Leu¹⁹¹ determines Inv (1, 2); Ala¹⁵³, Val¹⁹¹ determines Inv (3); and Val¹⁵³, Leu¹⁹¹ determines Inv (1). The Val¹⁵³, Val¹⁹¹ sequence has not been observed. It may correspond to Inv (–). These data are strikingly similar to the data for the Kern and Oz isotypes (changes at 154 and 191, respectively) in the chain. As in the case of theK chain, only three of the four possible combinations have been observed. The implications of this parallelism and of crystallographic findings on chains, reported by others, are discussed.     

An application of diagonal electrophoresis to the selective purification of serine phosphate peptides. Serine phosphate peptides from ovalbumin

A diagonal-electrophoresis method for the selective purification of serine phosphate peptides was applied to tryptic, chymotryptic and peptic digests of oxidized ovalbumin. This method is based on the release of the phosphate group bound to serine by treatment with alkaline phosphatase on paper. The identified serine phosphate peptides were purified by paper electrophoresis at pH6.5 and 2.0, dephosphorylation with bacterial alkaline phosphatase, and paper electrophoresis at pH2.0 again, in that order. The presence of two groups of serine phosphate peptides was apparent from the amino acid composition. One group contained no lysine, cysteic acid, proline, leucine or isoleucine (sequence 1) and the other had all those amino acids (sequence 2). Further degradation with subtilisin of those peptides and ;dansyl'-Edman sequence analysis established their partial sequences. The proposed sequences are as follows (with ;SerP' representing serine phosphate): sequence 1, -Ala-Gly-Arg-Glu-Val-Val-Gly-SerP-Ala-Glu-Ala-Gly-Asp-Val-Ala-Ala-Ser-(Val,Glx(2),Ser,Phe)-Arg-; sequence 2, -Asp-Lys-Leu-Pro-Gly-Phe-Gly-Asp-SerP-Ile-Glx-Ala-Glx-CySO(3)H-Gly-(Thr,Ser,Val)-(Asp,His,Val)-. The partial sequence of one of the phosphopeptides, Asp-(Glu,Ile,SerP), reported by Flavin (1954) was used to establish the proposed sequence 2.     

Immunoglobulin λ-chains. The complete amino acid sequence of a Bence-Jones protein

The total amino acid sequence of a lambda Bence-Jones protein has been established. The protein contains 211 residues, which include two methionine residues. Splitting with cyanogen bromide gave three fragments, the largest of which included the C-terminal half, which is common to other Bence-Jones proteins of the same type. The peptides obtained by tryptic, chymotryptic and peptic digestion were isolated and purified by paper-electrophoretic and chromatographic techniques. Reduction followed by carboxymethylation of the cysteine residues with radioactive iodoacetate was found to be a powerful tool in the isolation of some insoluble peptides. Unusual features of the molecule are the fact that it contains six cysteine residues and not five as observed in both kappa and lambda Bence-Jones proteins studied previously, and its size, which seems two residues smaller than the smallest Bence-Jones protein studied hitherto. The similarities and differences between this and other Bence-Jones proteins are discussed.     

Esters of serine and threonine in hydrolysates of histones and protamines, and attendant errors in amino acid analyses of proteins

1. Partial acid hydrolysates of histones from various origins and of protamine were analysed by a two-dimensional ionophoretic procedure to reveal strongly acidic ninhydrin-positive components. 2. Histone fractions prepared by extraction with sulphuric acid gave rise to spots identified as serine O-sulphate and threonine O-sulphate. These two compounds, which were not found in hydrolysates of corresponding fractions prepared by extraction with hydrochloric acid, were artifacts. 3. Hydrolysis of proteins in the presence of traces of sulphate can lead to the formation of the O-sulphates of serine and threonine. This can cause errors, which may sometimes be serious, in amino acid analyses of proteins. 4. O-Phosphoserine was obtained in small amounts from some histone fractions and from protamine, but was undetectable in other histone fractions, notably those of lower lysine content.     

Isolation of Aulacomya paramyosin

Tropomyosin A or paramyosin has been isolated from the adductor muscle of Aulacomya magellanica. It has in common with other tropomyosins A the method used for extracting it from adductor muscle, its solubility, facility of crystallization, ammonium sulphate range of precipitation, amino acid composition and behaviour when digested with trypsin. As a particular feature it exhibits an unusual low viscosity for this type of tropomyosin. Its molecular weight, determined by the Archibald approach-to-sedimentation-equilibrium method, is 258000+/-16000.     

Fungal biodegradation of lignopolystyrene graft copolymers.

White rot basidiomycetes were able to biodegrade styrene (1-phenylethene) graft copolymers of lignin containing different proportions of lignin and polystyrene [poly(1-phenylethylene)]. The biodegradation tests were run on lignin-styrene copolymerization products which contained 10.3, 32.2, and 50.4% (wt/wt) lignin. The polymer samples were incubated with the white rot fungi Pleurotus ostreatus, Phanerochaete chrysosporium, and Trametes versicolor and the brown rot fungus Gloeophyllum trabeum. White rot fungi degraded the plastic samples at a rate which increased with increasing lignin content in the copolymer sample. Both polystyrene and lignin components of the copolymer were readily degraded. Polystyrene pellets were not degradable in these tests. Degradation was verified for both incubated and control samples by weight loss, quantitative UV spectrophotometric analysis of both lignin and styrene residues, scanning electron microscopy of the plastic surface, and the presence of enzymes active in degradation during incubation. Brown rot fungus did not affect any of the plastics. White rot fungi produced and secreted oxidative enzymes associated with lignin degradation in liquid media during incubation with lignin-polystyrene copolymer.